Mechanism of maturation and nature of carbohydrate chains of boar sperm acrosin

FEBS Letters

Tesarik, J.¹  Leca, G.²  Peknicova, J.³  Moos, J.³ 

[1] Aster Biotechnologies, Les Nertierres, Allee H. Pintus, 06610 La Gaude, France;INSERM, Unite 131, 32 Rue des Carnets, 92140 Clamart, France;Institute of Molecular Genetics, Vídeňská 1083, Praha 4, 142 20, Czechoslovakia

关键词: Proacrosin activation;    Acrosin conversion;    Glycosylation;    Carbohydrate structure;    Boar spermatozoa;    SDS-PAGE;    sodium dodecylsulfate gel electrophoresis;   

DOI  :  10.1016/0014-5793(91)81335-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The acrosin zymogen proacrosin exists in two molecular forms which are believed to be single-chain polypeptides. During autoactivation in a cell-free system, the 55 and 53 kDa zymogens are sequentially converted into the 49, 36, 31 and 25 kDa forms. A similar mechanism of maturation was revealed, when the calcium ionophore A23187 was added to suspensions of boar spermatozoa. The 49 kDa form has been identified as the first active acrosin form in the maturation cascade. However, this form is indistinguishable from the 53 kDa zymogen in SDS-PAGE at nonreducing conditions. Two carbohydrate chains were evidenced on the acrosin molecule. The chain attached to the Asn³ of the acrosin light chain was enzymatically cleaved without loss of acrosin activity. By contrast, the carbohydrate chain linked to the acrosin heavy chain could be cleaved only after acrosin denaturation. Based on the susceptibility of acrosin to endoglycosidases F and H, a biantennary structure of both carbohydrate chains is proposed.

【 授权许可】

Unknown