Semisynthetic Peptides and Protein

References

• Gutte B., Merrifield R. B. The total synthesis of an enzyme with ribonuclease A activit. J. Am. Chem. Soc. 1969; 91: 501
   PubMed Web of Science ®Google Scholar
• Hirschmann R., Nutt R. F., Veber D. F., Vitali R. A., Varga S. L., Jacob T. A., Holly F. W., Denkewalter R. G. Studies of the total synthesis of an enzyme. V. The preparation of enzymically active materia. J. Am. Chem. Soc. 1969; 91: 507
   PubMed Web of Science ®Google Scholar
• Yajima H., Fujii N. Chemical synthesis of bovine pancreatic ribonuclease . J.C.S. Chem. Commun. 1980; 115
   Google Scholar
• Chaiken I. M. Engineering and characterization of semisynthetic ribonuclease-S′ sequence variant. Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 349
   Google Scholar
• Smythe D. G. Constructing semisynthetic polypeptide. Nature 1975; 256: 699
   Web of Science ®Google Scholar
• Semisynthetic Peptides and Proteins, R. E. Offord, C. Dibello. Academic Press, London 1978
   Google Scholar
• Sheppard R. C. Partial synthesis of peptides and protein. The Peptides, E. Gross, J. Meienhofer. Academic Press, New York 1980; Vol. 2: 441
   Google Scholar
• Offord R. E. Semisynthetic Proteins. John Wiley & Sons, Chichester 1980
   Google Scholar
• Peptides — Structure and Biological Function, E. Gross, J. Meienhofer. Pierce Chem. Co., Rockford, Ill 1979
   Google Scholar
• Methods in Enzymology, C. H. W. Hirs. Academic Press, New York 1971; Vol. II
   Google Scholar
• Methods in Enzymology, C. H. W. Hirs, S. N. Timasheff. Academic Press, New York 1972; Vol. 25
   Google Scholar
• Methods in Enzymology, C. H. W. Hirs, S. N. Timasheff. Academic Press, New York 1977; Vol. 47
   Google Scholar
• Methods in Enzymology, G. E. Perlmann, L. L. Lorand. Academic Press, New York 1970; Vol. 19
   Google Scholar
• Methods in Enzymology, L. Lorand. Academic Press, New York 1976; Vol. 45
   Google Scholar
• Tesser G. I., Balvert-Geers I. C. The methylsulfonylethoxycarbonyl group, a new and versatile amino protective functio. Int. J. Pept. Prot. Res. 1975; 7: 297
   Google Scholar
• Goldberger R. F., Anfinsen C. B. The reversible masking of amino groups in ribonuclease and its possible usefulness in the synthesis of the protei. Biochemistry 1962; 1: 401
   Web of Science ®Google Scholar
• Hunter M. L., Ludwig M. J. The reaction of imidoesters with proteins and related small molecule. J. Am. Chem. Soc. 1962; 84: 3491
   Web of Science ®Google Scholar
• Mitchell W. M., Harrington W. F. Purification and properties of clostridopeptidase B (clostripain. J. Biol. Chem. 1968; 243: 4683
   PubMed Web of Science ®Google Scholar
• Taniuchi T., Anfinsen C. B., Sodja A. Nuclease-T: an active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragment. Proc. Natl. Acad. Sci. U.S.A. 1967; 58: 1235
   PubMed Web of Science ®Google Scholar
• Richards F. M., Vithayathil P. J. The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein component. J. Biol. Chem. 1959; 234: 1459
   PubMed Web of Science ®Google Scholar
• Gross E., Witkop B. Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromid. J. Am. Chem. Soc. 1961; 83: 1510
   Web of Science ®Google Scholar
• Corradin G., Harbury H. A. Reconstitution of horse heart cytochrome c: interaction of the components obtained upon cleavage of the peptide bond following methionine 6. Proc. Nail. Acad. Sci. U.S.A. 1971; 68: 3036
   PubMed Web of Science ®Google Scholar
• Boon P. J., Tesser G. I., Nivard R. J. F. Semisynthetic horse heart [65-homoserine]cytochrome c from three fragment. Proc. Natl. Acad. Sci. U.S.A. 1979; 76: 61
   PubMed Web of Science ®Google Scholar
• Wallace C. J. A., Offord R. E. The semisynthesis of fragments corresponding to residues 66–104 of horse heart cytochrome . Biochem. J. 1979; 179: 169
   PubMed Web of Science ®Google Scholar
• Ledden D. J., Nix P. T., Warme P. K. Protected natural peptides as intermediates for preparing semisynthetic peptides and protein analogs — selective acylation of α-amino groups in cyanogen bromide peptides of cytochrome using azidoformate. Biochim. Biophys. Acta 1979; 578: 401
   PubMedGoogle Scholar
• Dyckes D. F., Creighton T., Sheppard R. C. Spontaneous re-formation of a broken peptide chai. Nature 1974; 247: 202
   PubMed Web of Science ®Google Scholar
• Omenn G. S., Fontana A., Anfinsen C. B. Modification of the single tryptophan residue of staphylococcal nuclease by a new mild oxidizing agen. J. Biol. Chem. 1970; 245: 1895
   PubMed Web of Science ®Google Scholar
• Mahoney W. C., Hermodson M. A. High-yield cleavage of tryptophanyl peptide bonds by o-iodosobenzoic aci. Biochemistry 1979; 18: 3810
   PubMed Web of Science ®Google Scholar
• Fontana A., Savige W. E., Zambonin M. Advances in the chemical cleavage of tryptophanyl peptide bond. Methods in Peptide and Protein Sequence Analysis, C. Birr. Elsevier/North-Holland, Amsterdam 1980; 309
   Google Scholar
• Jacobson G. R., Schaffer M. H., Stark G. R., Vanaman T. C. Specific chemical cleavage in high yield at the amino peptide bonds of cysteine and cystin. J. Biol. Chem. 1973; 248: 6583
   PubMed Web of Science ®Google Scholar
• Degani Y., Patchornik A. Cyanylation of sulfhydryl groups by 2-nitro-5-thiocyanobenzoic acid. High-yield modification and cleavages of peptides at cysteine residue. Biochemistry 1974; 13: 1
   PubMed Web of Science ®Google Scholar
• Lin M. C., Gutte B. Moore, S. and Merrifield, R. B., Regeneration of activity by mixture of ribonuclease enzymatically degraded from the COOH terminus and a synthetic COOH-terminal tetradecapeptid. J. Biol. Chem. 1970; 245: 5169
   PubMed Web of Science ®Google Scholar
• Anfinsen C. B. The limited digestion of ribonuclease with pepsi. J. Biol. Chem. 1956; 221: 405
   PubMed Web of Science ®Google Scholar
• Andria G., Taniuchi H. The complementary fragment-dependent renaturation by enzyme-catalyzed disulfide interchange of RNase-(1–118) containing non-native disulfide bond. J. Biol. Chem. 1978; 253: 2262
   PubMed Web of Science ®Google Scholar
• Juillerat M., Parr G. R., Taniuchi H. A biologically active, three-fragment complex of horse heart cytochrome . J. Biol. Chem. 1980; 255: 845
   PubMed Web of Science ®Google Scholar
• Merrifield R. B., Kent S. B. H., Tarn J. P., Tjoeng F. S., Sarin V., Mojsov S., Riemen M. W., Wong T. W., Voss C. Solid phase peptide synthesi. Peptides — Structure and Biological Function, E. Gross, J. Meienhofer. Pierce Chem. Co., Rockford 1979; 111: 29
   Google Scholar
• Mitchell A. R., Kent S. B. H., Englehard M., Merrifield R. B. A new synthetic route to tert-butyl-oxycarbonylaminoacyl-4-(oxymethyl)-phenylacetamidomethyl-resin, an improved support for solid phase peptide synthesi. J. Org. Chem. 1978; 43: 2845
   Web of Science ®Google Scholar
• Komoriya A., Homandberg G. A., Chaiken I. M. Enzyme-catalyzed formation of semisynthetic staphylococcal nuclease using a new synthetic fragment, [48-glycine]synthetic-(6–49. Int. J. Pept. Prot. Res. 1980; 16: 433
   PubMedGoogle Scholar
• Ontjes D. A., Anfinsen C. B. Solid phase synthesis of a 42-residue fragment of staphylococcal nuclease: properties of a semisynthetic enzym. Proc. Natl. Acad. Sci. U.S.A. 1969; 64: 428
   PubMed Web of Science ®Google Scholar
• Chaiken I. M. Purification and properties of semisynthetic staphylococcal nuclease-T′. J. Biol. Chem. 1971; 246: 2948
   PubMed Web of Science ®Google Scholar
• Atherton E., Clive D. I. J., Sheppard R. C. Polyamide supports for polypeptide synthesi. J. Am. Chem. Soc. 1975; 97: 6584
   PubMed Web of Science ®Google Scholar
• Sparrow J. T. An improved polystyrene support for solid phase peptide synthesi. J. Org. Chem. 1976; 41: 1350
   PubMed Web of Science ®Google Scholar
• Kalir C., Warshawsky A., Fridkin M., Patchornik A. New useful reagents for peptide synthesis. Insoluble active esters of polystyrene-bound 1-hydroxybenzatriazol. Eur. J. Biochem. 1975; 39: 55
   Google Scholar
• Chaiken I. M. Functional purification of synthetic proteins and protein fragment. Methods in Enzymology, W. B. Jakoby, M. Wilchek. Academic Press, New York 1974; Vol. 37: 631
   Google Scholar
• Hansen J. J., Greibrokk T., Currie B. L., Johannsson K. N.-G., Folkers K. High-pressure liquid chromatography of peptide. J. Chromatogr. 1977; 135: 155
   PubMed Web of Science ®Google Scholar
• Rivier J. E. Use of trialkyl ammonium phosphate (TAAP) buffers in reverse phase HPLC for high resolution and high recovery of peptide and protein. J. Liquid Chromatogr. 1978; 1: 343
   Web of Science ®Google Scholar
• Taniuchi H., Anfinsen C. B. An experimental approach to the study of the folding of staphylococcal nucleas. J. Biol. Chem. 1969; 244: 3864
   PubMed Web of Science ®Google Scholar
• Harris D. E., Offord R. E. A functioning complex between tryptic fragments of cytochrome c — a route to the production of semisynthetic analogue. Biochem., J. 1977; 161: 21
   PubMed Web of Science ®Google Scholar
• Parr G. R., Hantgan R. R., Taniuchi H. Formation of two alternative complementing structures from a cytochrome c heme fragment (residue 1 to 38) and to the apoprotei. J. Biol Chem. 1978; 253: 5381
   PubMed Web of Science ®Google Scholar
• Li C. H., Bewley T. A. Human pituitary growth hormone: restoration of full biological activity by non-covalent interaction of two fragments of the hormon. Proc. Natl. Acad. Sci. U.S.A. 1976; 73: 1476
   PubMed Web of Science ®Google Scholar
• Hartley R. W. Complementation of peptides of barnase, extracellular ribonuclease o. Bacillus amyloliquefaciens, J. Biol. Chem. 1977; 252: 3252
   PubMed Web of Science ®Google Scholar
• Wang C.-C., DiMarchi R. D., Gurd F. R. N. Replacement of the N-terminal tetradecapeptide sequence of sperm whale myoglobin, in Ref. 6, 6. Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 60
   Google Scholar
• Hagenmaier H., Ohms J. P., Jahns J., Anfinsen C. B. Studies on the semisynthesis of myoglobin from natural fragment. Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 23
   Google Scholar
• Slotboom A. J., De Haas G. H. Specific transformations at the N-terminal region of phospholipase A2. Biochemistry 1975; 14: 5394
   PubMed Web of Science ®Google Scholar
• Ruttenberg M. A. Human insulin: facile synthesis by modification of porcine insuli. Science 1972; 177: 623
   PubMed Web of Science ®Google Scholar
• Geiger R., Obermeier R. Contribution of peptide chemistry to our knowledge of insulin and diabete. Proinsulin, Insulin, and C-peptide, S. Baba, T. Kaneko, N. Yanaihara. Excerpta Medica, Amsterdam 1979; 62
   Google Scholar
• Corradin G., Harbury H. A. Reconstitution of horse heart cytochrome c: reformation of the peptide bond linking residues 65 and 6. Biochem. Biophys. Res. Commun. 1974; 61: 1400
   PubMed Web of Science ®Google Scholar
• Homandberg G. A., Laskowski M., Jr. Enzymatic resynthesis of the hydrolyzed peptide bond(s) in ribonuclease . Biochemistry 1979; 18: 586
   PubMed Web of Science ®Google Scholar
• Laskowski M., Jr. The use of proteolytic enzymes for the synthesis of specific peptide bonds in globular protein. Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 256
   Google Scholar
• Kowalski D. Replacements, insertions, and modifications of amino acid residues in the reactive site of soybean trypsin inhibitor (kunitz. Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 263
   Google Scholar
• Jering H., Tschesche H. Amino acid replacement at the reactive site of the bovine trypsin-kallikrein inhibitor (kunitz. Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 283
   Google Scholar
• Inouye K., Watanabe K., Morihara K., Tochino Y., Kanaya T., Emura J., Sakakibara S. Enzyme-assisted semisynthesis of human insuli. J. Am. Chem. Soc. 1979; 101: 751
   Web of Science ®Google Scholar
• Homandberg G. A., Chaiken I. M. Trypsin-catalyzed conversion of staphylococcal nuclease-T fragment complexes to covalent form. J. Biol. Chem. 1980; 255: 4903
   PubMed Web of Science ®Google Scholar
• Homandberg G. A., Komoriya A., Juillerat M., Chaiken I. M. Enzymatic conversion of selected noncovalent complexes of native or synthetic fragments to covalent form. Peptides — Structure and Biological Function, E. Gross, J. Meienhofer. Pierce Chem. Co., Rockford, Ill 1979; 597
   Google Scholar
• Komoriya A., Homandberg G. A., Chaiken I. M. Enzymatic fragment condensation using kinetic trap. Peptides 1980, K. Brunfeldt. Scriptor Press, Copenhagen 1981; 378
   Google Scholar
• Edman P. Preparation of phenyl thiohydantoins from some natural amino acid. Acta Chem. Scand. 1950; 4: 277
   Google Scholar
• Widmer F., Johansen J. T. Enzymatic peptide synthesis. Carboxypeptidase Y catalyzed formation of peptide bond. Carlsberg Res. Commun. 1979; 44: 37
   Google Scholar
• Hofmann K., Visser J. P., Finn F. M. Studies of polypeptides. XLIII. Synthesis of S-peptide 1–20 by two route. J. Am. Chem. Soc. 1969; 91: 4883
   PubMed Web of Science ®Google Scholar
• Scoffone F., Marchiori F., Rocchi R., Vidal G., Tamburro A., Scatturin A., Marzotto A. Synthesis of an enzymatically active orn10-S-peptide of ribonuclease-. Tetrahedron Lett. 1966, No. 9: 943
   PubMed Web of Science ®Google Scholar
• Pandin M., Padlan E. A., DiBello C., Chaiken I. M. Crystalline semisynthetic ribonuclease-S′. Proc. Natl. Acad. Sci. U.S.A. 1976; 73: 1844
   PubMed Web of Science ®Google Scholar
• Hayaishi R., Moore S., Merrifield R. B. Preparation of pancreatic ribonuclease 1–114 and 1–115 and their reactivation with synthetic COOH-terminal peptide. J. Biol. Chem. 1973; 248: 3889
   PubMed Web of Science ®Google Scholar
• Sheppard R. C. Selected chain cleavage and combination in protein partial synthesi. Peptides — Structure and Biological Function, E. Gross, J. Meienhofer. Pierce Chem. Co., Rockford, Ill 1979; 577
   Google Scholar
• Parikh I., Corley L., Anfinsen C. B. Semisynthetic analogues of an enzymically active complex formed between two overlapping fragments of staphylococcal nucleas. J. Biol. Chem. 1971; 246: 7392
   PubMed Web of Science ®Google Scholar
• Barstow L. E., Young R. S., Yakali E., Sharp J. J., O'Brien J. C., Berman P. W., Harbury H. A. Semisynthetic cytochrome . Proc. Natl. Acad. Sci. U.S.A. 1977; 74: 4248
   PubMed Web of Science ®Google Scholar
• Nix P. T., Warme P. K. Semisynthetic analogs of cytochrome c reconstructed from natural and synthetic peptide. Biochim. Biophys. Acta 1979; 578: 413
   PubMed Web of Science ®Google Scholar
• Harris D. E. Cytochrome c-T: a functioning complex between tryptic fragments of cytochrome c and its use in the preparation of semisynthetic analogues of cytochrome c modified at positions 38 and 3. Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 127
   Google Scholar
• Juillerat M., Taniuchi H. Personal communication 1980
   Google Scholar
• DiMarchi R. D., Neireiter G. W., Garner W. H., Gurd F. R. N. Myoglobin semisynthesis: removal of the NH2-terminal valine of sperm whale myoglobin and its subsequent reincorporatio. Biochemistry 1979; 18: 3101
   PubMed Web of Science ®Google Scholar
• Katsoyannis P. G., Trakatellis A. C., Zalut C., Johnson S., Tometsko A., Schwartz G., Ginos J. Studies on the synthesis of insulin from natural and synthetic A and B chains. III. Synthetic insulin. Biochemistry 1967; 6: 2656
   PubMed Web of Science ®Google Scholar
• Li C. H., Bewley T. A., Blake J., Hayashida T. Human somatotropin: restoration of full biological activity by noncovalent interaction of a natural and a synthetic fragment of the hormon. Proc. Natl Acad. Sci. U.S.A. 1977; 74: 1016
   PubMed Web of Science ®Google Scholar
• Boon P. J., Tesser G. I., Nivard R. J. F. Semisynthesis of [HSer 65] cytochrome . Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 115
   Google Scholar
• Van Nispen J. W., Smeets P. J. H., Poll E. H. A., Tesser G. I. Investigation of the role of tryptophan in α-MS. Int. J. Pept. Prot. Res. 1977; 9: 203
   PubMedGoogle Scholar
• Burton J., Lande S. Semisynthetic polypeptides. Transformation of native porcine β-melanotropin into the lysine-10 analog of the human hormon. J. Am. Chem. Soc. 1970; 92: 3746
   PubMed Web of Science ®Google Scholar
• Gavish M., Zakut R., Wilchek M., Givol D. Preparation of a semisynthetic antibod. Biochemistry 1978; 17: 1345
   PubMedGoogle Scholar
• Lode E. T., Murray C. L., Sweeney W. V., Rabinowitz J. C. Synthesis and properties of Clostridium acidi-urici [Leu2]-ferredoxin: a function of the peptide chain and evidence against the direct role of the aromatic residues in electron transfe. Proc. Natl. Acad. Sci. U.S.A. 1974; 71: 1361
   PubMedGoogle Scholar
• Rees A. R., Offord R. E. The semisynthesis of portions of hen's-egg lysozyme by fragment condensatio. Biochem. J. 1976; 159: 487
   PubMed Web of Science ®Google Scholar
• Fölsch G. Semisynthetic work on human carbonic anhydrase . Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 309
   Google Scholar
• Borrás-Cuesta F., Pavani M., Romo D., Malebran P. Preliminary studies on the semisynthesis of myoglobi. Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 37
   Google Scholar
• Borrás-Cuesta F., Offord R. E. Protected intermediate for the preparation of semisynthetic insulin. Nature 1970; 227: 717
   Web of Science ®Google Scholar
• Finn F. M., Hofmann K. The S-peptide-S-protein system: a model for hormone-receptor interactio. Accts. Chem. Res. 1973; 6: 169
   Web of Science ®Google Scholar
• Scoffone E., Marchiori F., Moroder L., Rocchi R., Borin G. Synthesis and biological properties of S-peptide analog. Medicinal Chemistry III, Milan, Special Contributions, P. Pratesi. Butterworths, London 1973; 83
   Google Scholar
• Dunn B. M., Chaiken I. M. Relationship between α-helical propensity and formation of the ribonuclease-S comple. J. Mol. Biol. 1975; 95: 497
   PubMed Web of Science ®Google Scholar
• Chaiken I. M., Taylor H. C., Ammon H. L. Crystal properties of [des 16–20]semisynthetic sequence variants of ribonuclease . J. Biol. Chem. 252, 5599
   Web of Science ®Google Scholar
• Van Batenburg O. D., Raap J., Kerling K. E. T., Havinga E. A partially synthetic highly active ribonuclease S analogue in which L-homohistidine replaces histidine-12 as the operative componen. Tetrahedron Lett. 1975, No. 51: 4591
   Web of Science ®Google Scholar
• Levit S., Berger A. Ribonuclease S-peptide. A model for molecular recognitio. J. Biol Chem. 1976; 251: 1333
   PubMed Web of Science ®Google Scholar
• Dunn B. M., DiBello C., Kirk K., Cohen L. A., Chaiken I. M. Synthesis, purification, and properties of a semisynthetic ribonuclease S incorporating 4-fluoro-L-histidine at position 1. J. Biol. Chem. 1974; 249: 6295
   PubMed Web of Science ®Google Scholar
• Chaiken I. M., Freedman M. H., Lyerla J. R., Jr., Cohen J. S. Preparation and studies of 19F-labeled and enriched 13C-labeled semisynthetic ribonuclease-S′ analogue. J. Biol. Chem. 1973; 248: 884
   PubMed Web of Science ®Google Scholar
• Taylor H. C., Chaiken I. M. Active site ligand binding by an inactive ribonuclease S analogue. A quantitative affinity chromatographic stud. J. Biol. Chem. 1977; 252: 6991
   PubMed Web of Science ®Google Scholar
• Filippi B., Borin G., Marchiori F. The influence of amino acid side-chains on α-helix stability: S-peptide analogues and related ribonucleases S′. J. Mol Biol. 1976; 106: 315
   PubMed Web of Science ®Google Scholar
• Hofmann K., Visser J. P., Finn F. M. Studies on polypeptides. XLIV. Potent synthetic S-peptide antagonist. J. Am. Chem. Soc. 1970; 92: 2900
   PubMed Web of Science ®Google Scholar
• Chaiken I. M., Komoriya A., Homandberg G. P. Protein semisynthesis and the chemical basis of folding and functio. Peptides — Structure and Biological Function, E. Gross, J. Meienhofer. Pierce Chem. Co., Rockford, Ill 1979; 587
   Google Scholar
• Van Batenburg O. D., Kerling K. E. T., Havinga E. Synthesis and enzymatic activity of an RNase S′ analogue in which the 4-imidazolylglycyl residue takes the position and the role of histidine 1. FEBS Lett. 1976; 68: 228
   PubMed Web of Science ®Google Scholar
• Van Batenburg O. D., Kerling K. E. T., Havinga E. Studies on polypeptides. XVIII. Solid-phase synthesis of RNase S-peptide analogues with high S-protein activating ability; replacement of histi-dine-12 by L-homohistidin. Rec. Trav. Chim. Pays-Bas 1976; 95: 278
   Google Scholar
• Finn F. M., Visser J. B., Hofmann K. Structure-function studies in partially synthetic ribonucleas. Peptides 1968, E. Bricas. North-Holland, Amsterdam 1968; 330
   Google Scholar
• Borin G., Toniolo C., Moroder L., Marchiori F., Rocchi R., Scoffone E. Synthesis of peptide analogs of the N-terminal eicosapeptide sequence of ribonuclease . Int. J. Pept. Prot. Res. 1972; 4: 37
   Google Scholar
• Komoriya A., Krigbaum W. R., Chaiken I. M. On the chemical information required in S-peptide for the conformational stabilization of ribonuclease-. Peptides 1978, I. Z. Siemion, G. Kupryszewski. Wroclaw University Press, Warsaw 1979; 657
   Google Scholar
• Wyckoff H. W., Tsernoglou D., Hanse A. W., Knox J. R., Lee B., Richards F. M. The three-dimensional structure of ribonuclease-S. interpretation of an electron density map at a nominal resolution of 2. J. Biol. Chem. 1970; 245: 305
   PubMed Web of Science ®Google Scholar
• Taylor H. C., Richardson D. C., Richardson J. S., Wlodawer A., Komoriya A., Chaiken I. M. J. Mol. Biol., in press
   Google Scholar
• Richards F. M., Wyckoff H. W. Bovine pancreatic ribonucleas. The Enzymes, 3rd ed., P. D. Boyer. Academic Press, New York 1971; Vol. 4: 647
   Google Scholar
• Chaiken I. M., Komoriya A. Protein semisynthesi. Trends Biochem. Sci. 1978; 3: 269
   Google Scholar
• Lenstra J. A., Hofsteenge J., Beintema J. J. Invariant features of the structure of pancreatic ribonuclease. A test of different predictive model. J. Mol. Biol. 1977; 109: 185
   PubMed Web of Science ®Google Scholar
• Voskuyl-Holtkamp I., Shattenkerk C. Studies on polypeptides. XXI. Synthesis of four protected peptide fragments corresponding to parts of the N-terminal 1–17 sequence of rat pancreatic ribonucleas. Int. J. Pept. Prot. Res. 1977; 10: 60
   PubMedGoogle Scholar
• Voskuyl-Holtkamp I., Shattenkerk C. Studies on polypeptides. XXIV. Synthesis of the 5–17 and 1–17 peptide sequences of rat ribonucleas. Int. J. Pept. Prot. Res. 1977; 10: 153
   PubMedGoogle Scholar
• Vithayathil P. S., Richards F. M. Modification of the methionine residue in the peptide component of ribonuclease-. J. Biol Chem. 1960; 235: 2343
   Web of Science ®Google Scholar
• Krigbaum W. R., Komoriya A. Local interactions as a structure determinant for protein molecules: II. Biochim. Biophys. Acta 1979; 576: 229
   PubMedGoogle Scholar
• Vithayathil P. J., Richards F. M. Modification of the amino groups of the peptide component of subtilisin-modified ribonucleas. J. Biol. Chem. 1960; 235: 1029
   Web of Science ®Google Scholar
• Halban P. A., Karakash C., Davies J. G., Offord R. E. The degradation of semisynthetic tritiated insulin by perfused mouse liver. Biochem. J. 1976; 160: 409
   PubMed Web of Science ®Google Scholar
• Taniuchi H. The dynamic equilibrium of folding and unfolding of nuclease-T′. J. Biol. Chem. 1978; 248: 5164
   Google Scholar
• Chaiken I. M. Carbon 13 as a probe of helix formation in semisynthetic ribonuclease-S′. J. Biol. Chem. 1974; 249: 1247
   PubMed Web of Science ®Google Scholar
• Niu C.-H., Matsuura S., Shindo H., Cohen J. S. Specific peptide-protein interactions in the ribonuclease S′ system studied by 13C nuclear magnetic resonance spectroscopy with selectively 13C-enriched peptide. J. Biol. Chem. 1979; 254: 3788
   PubMed Web of Science ®Google Scholar
• Chaiken I. M., Cohen J. S., Sokoloski E. A. Microenvironment of histidine 12 in ribonuclease-S as detected by 12C nuclear magnetic resonanc. J. Am. Chem. Soc. 1974; 95: 4703
   Google Scholar
• Paolillo L., Tancredi T., Temussi D. A., Trivellone E., Bradbury E. M., Crane-Robinson C. The helix-coil transition of poly-(γ-benzyl-L-glutamate) using 13C resonance spectroscop. J. Chem. Soc. D. Chem. Commun. 1972; 335
   Google Scholar
• Boccalon G., Verdini A. S., Giacometti G. Helix-coil transition of a synthetic polypeptide monitored by fourier transform carbon 13 nuclear magnetic resonanc. J. Am. Chem. Soc. 1972; 94: 3639
   PubMed Web of Science ®Google Scholar
• Chaiken I. M., Dunn B. M. Semisynthetic 13C-enriched and 19F-labeled peptide-protein non-covalent complexe. Peptides 1974, Y. E. Wolman. John Wiley & Sons, New York 1975; 299
   Google Scholar
• Gutte B., Lin M. C., Caldi D. G., Merrifield R. B. Reactivation of des (119-, 120-, or 121–124) ribonuclease A by mixture with synthetic COOH-terminal peptides of varying length. J. Biol. Chem. 1972; 247: 4765
   Web of Science ®Google Scholar
• Lin M. C., Gutte B., Caldi D. G., Moore S., Merrifield R. B. Reactivation of des (119–124) ribonuclease A by mixture with synthetic COOH-terminal peptides; the role of phenylalanine-12. J. Biol. Chem. 1972; 247: 4768
   PubMed Web of Science ®Google Scholar
• Chaiken I. M. Chemical studies of structural features in staphylococcal nuclease-T′. J. Biol. Chem. 1972; 247: 1995
   Web of Science ®Google Scholar
• Chaiken I. M., Anfinsen C. B. A solid phase synthetic study of the active site region of staphylococcal nuclease-. J. Biol. Chem. 1971; 246: 2285
   PubMed Web of Science ®Google Scholar
• Chaiken I. M., Sanchez G. R. Active site properties of [aspartic acid 43]semisynthetic nuclease-T′. J. Biol. Chem. 1972; 247: 6743
   PubMed Web of Science ®Google Scholar
• Sánchez G. R., Chaiken I. M., Anfinsen C. B. Structure-function relationships at the active site of nuclease-T′. J. Biol. Chem. 1973; 248: 3653
   PubMed Web of Science ®Google Scholar
• Arnone A., Bier C. J., Cotton F. A., Day V. W., Hazen E. E., Jr., Richardson D. C., Richardson J. S., Yonath A. A high resolution structure of an inhibitor complex of the extracellular nuclease of Staphylococcus aureus. I. Experimental procedures and chain tracin. J. Biol. Chem. 1971; 246: 2302
   PubMed Web of Science ®Google Scholar
• Chaiken I. M., Anfinsen C. B. A solid phase synthetic study of structure-function relationships in the amino-terminal region of staphylococcal nucleas. J. Biol. Chem. 1970; 245: 4718
   PubMed Web of Science ®Google Scholar
• Fölsch G., Nyman P. O., Strid L. Personal communication 1980
   Google Scholar
• Webster D., Offord R. E. The modification and removal of the N-terminal residue of trypsin by transaminatio. Biochem. J. 1972; 130: 315
   PubMed Web of Science ®Google Scholar
• Slotboom A. J., Jansen E. H. J. M., Pattus F., De Haas G. H. Semisynthetic studies on phospholipase A2. Semisynthetic Peptides and Proteins, R. E. Offord, C. DiBello. Academic Press, London 1978; 315
   Google Scholar
• Pattus F., Slotboon A. J., De Haas G. H. Amino acid substitutions at the NH2-terminal Ala1 of porcine pancreatic phospholipase A2: a monolayer stud. Biochemistry 1979; 18: 2703
   PubMed Web of Science ®Google Scholar
• Korb H., Neupert W. Biogenesis of cytochrome c in Neurospora crassa. Synthesis of apocytochrome c, transfer to mitochondria and conversion to holocytochrome . Eur. J. Biochem. 1978; 91: 609
   PubMedGoogle Scholar
• Basile G., DiBello C., Taniuchi H. Formation of an iso-l-cytochrome c-like species containing a covalently bonded heme group from the apoprotein by a yeast cell-free system in the presence of hemi. J. Biol. Chem. 1980; 255: 7181
   PubMed Web of Science ®Google Scholar
• Dickerson R. E., Timkovich R. Cytochromes . The Enzymes, 3rd Ed., P. D. Boyer. Academic Press, New York 1975; Vol. II: 397
   Google Scholar
• Wasserman G. F., Nix P. T., Koul A. K., Warme P. K. Semi-synthetic analogs of cytochrome c — substitutions for methionine at position 8. Biochim. Biophys. Acta 1980; 623: 457
   PubMed Web of Science ®Google Scholar
• Boon P. J., Van Raay A. J. M., Tesser G. I., Nivard R. J. F. Semisynthesis, conformation, and cytochrome c oxidase activity of eight cytochrome c analogue. FEBS Lett. 1979; 108: 131
   PubMed Web of Science ®Google Scholar
• Smith E. L. Evolution of enzyme. The Enzymes, 3rd ed., P. D. Boyer. Academic Press, New York 1970; Vol. I: 267
   Google Scholar
• Margoliash E., Fitch W. M., Markowitz E., Dickerson R. E. Functional limits of cytochrome c variabilit. Structure and Function of Oxidation-Reduction Enzymes, A. Akeson, A. Ehrenberg. Pergamon Press, Oxford 1972; 5
   Google Scholar
• DiMarchi R. D., Neireiter G. W., Heath W. F., Gurd F. R. N. Structural significance of the amino terminal residues of sperm whale myoglobi. Biochemistry 1980; 19: 2455
   Web of Science ®Google Scholar
• Carpenter F. H., Paynovich R. C., Yeung C. W.-T. Combination of the A and B chains of insuli. Peptides — Structure and Biological Function, E. Gross, J. Meienhofer. Pierce Chem. Co., Rockford, Ill 1979; 219
   Google Scholar
• Geiger R., Schone H.-H., Pfaff W. Bis (tert.-butyloxycarbonyl) insuli. Hoppe-Seyler's Z. Physiol. Chem. 1971; 352: 1487
   PubMedGoogle Scholar
• Naithani V. K., Gattner H.-G., Bullesbach E. E., Zahn H. Novel semisynthetic approaches to insulin and its precursor. Structural Studies on Molecules of Biological Interest, G. Dodson, J. Glusker, D. Sayre. Oxford University Press, Oxford, in press
   Google Scholar
• Burton J., Topper R., Ehrlich P. Semisynthesis of an antibody fragment: quantitation and correction of deletion sequence. Peptides — Structure and Biological Function, E. Gross, J. Meienhofer. Pierce Chem. Co., Rockford, Ill 1979; 605
   Google Scholar
• Morihara K., Oka T., Tsuzuki H. Semi-synthesis of human insulin by trypsin-catalysed replacement of ala-B30 by Thr in porcine insuli. Nature 1979; 280: 412
   PubMed Web of Science ®Google Scholar
• Genetic Engineering — Principles and Methods, J. K. Setlow, A. Hollaender. Plenum Press, New York 1979; Vol. 1 and 2, and 1980
   Google Scholar
• Goeddel D. V., Kleid D. G., Bolivar F., Heyneker H. L., Yansura D. G., Crea R., Hirose T., Kraszewski A., Itakura K., Riggs A. D. Expression in Escherichia coli of chemically synthesized genes for human insuli. Proc. Natl. Acad. Sci. U.S.A. 1979; 76: 106
   PubMed Web of Science ®Google Scholar
• Riggs A. D., Itakura K., Hirose T., Kraszewski A., Crea R., Goeddel D., Kleid D., Yansura D., Bolivar F., Heyneker H. Chemical DNA synthesis as an approach to peptide synthesis: the human insulin projec. Peptides — Structure and Biological Function, E. Gross, J. Meienhofer. Pierce Chem. Co., Rockford, Ill 1979; 985
   Google Scholar
• Itakura K., Hirose T., Crea R., Riggs A. D., Heyneker H. L., Bolivar F., Boyer H. W. Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostati. Science 1977; 198: 1056
   PubMed Web of Science ®Google Scholar
• Hutchison C. A., III, Phillips S., Edgell M. H., Gillam S., Jahnke P., Smith M. Mutagenesis at a specific position in a DNA sequenc. J. Biol. Chem. 1978; 251: 6551
   Google Scholar