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Abstract
Two bovine lutropin standard preparations (NIH-LH-B9, NIAMDD-bLH4) were applied on a recently developed anion-exchange column (Protein Pak DEAE 5PW,Waters Associates). The content of the eluted fractions was examined by a homologous radioimmunoassay of lutropin. In order to compare this fractionation with other independent methods, the two lutropin preparations were applied to SDS polyacrylamide gel eletrophoresis. The results indicate that the elution with a iris-hydrochloric acid buffer pH 6.5 allows within 2 minutes a convenient separation of the most LH immuno-reactive components of these preparations. Analysis on gel elect-rophoresis indicates that after fractionation on this anion-exchange column, some stained bands were removed from NIH-LH-B9 but not from NIAMDD-bLH-4.