In vitro effect of novel β-lactam compounds on xanthine oxidase enzyme activity

Figures & data

Figure 1. IC₅₀ graphics of β-lactam derivatives.

Table I. Effects of new β-lactam derivatives on the enzyme activity of a purified XO from bovine milk.

Lactams	R-	IC50 (μM)
3a	H	34.77
3b	4-CH3	47.42
3c	3-CH3	36.73
3d	4-OCH3	31.64
3e	3-OCH3	38.08
3f	4-Cl	21.65
3g	3-Cl	38.69
3h	4-NO2	32.79
3i	3-NO2	24.47
3j	2-NO2	30.37
3k	2-Br	58.04
3l	4-F	41.24

Table II. Summary of the purification procedure of milk xanthine oxidase.

Step	Volume (mL)	Activity (U/mL)	Total Activity |(U)	Protein Amount (mg/mL)	Total Protein (mg)	Specific Activity (U/mg)	Overall Yield (%)	Overall Purification (fold)
Milk	100	91.12	9112	4.31	431.25	21.13	100	–
Ammonium sulphate precipitation	12	125.31	1503.72	6.55	78.64	19.12	16.50	0. 90
Affinity chromatography	3.0	361.90	1085.7	0.093	0.28	1292.5	11.91	67.6

Figure 2. SDS-PAGE of xanthine oxidase. The poled fractions from affinity chromatography were analyzed by SDS-PAGE (12% and 3%) and revealed by Coomassie Blue staining. Experimental conditions were as described in the method. Lane 1 contained 5 μL of various molecular mass standards: 3-galactosidase, (116.0), bovine serum albumin (66.2), ovalbumin (45.0), lactate dehydrogenase (35.0), restriction endonuclease (25.0), 3-lactoglobulin (18.4), lysozyme (14.4). Only one protein-staining band was detectable on Line 2.