학술논문
Bull Semen Ribonucleases 1. Purification and Physico-Chemical Properties of the Major Component.
Document Type
Article
Source
Subject
*SEMINAL proteins
*AMINO acids
*CYSTEINE proteinases
*TRYPTOPHAN
*ENZYMES
*RIBONUCLEASES
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*
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Language
ISSN
0014-2956
Abstract
A high ribonuclease activity has been detected in bull seminal plasma; two major fractions (RNAase BS-1 and RNAase BS-2) have been identified, which are responsible for such activity and one of the two, RNAase BS-1, has been purified and crystallized. It has a molecular weight of 29000, an isoelectric point at pH 10.3 and A1 cm1% at 278 nm is 4.65. The amino acid composition has been determined, its main features being a high content of basic residues, the absence of tryptophan and cysteine, and the presence of 18 half-cystine residues. The enzyme is produced by the seminal vesicles, and occurs in seminal plasma as a free, soluble component. [ABSTRACT FROM AUTHOR]