The soluble hyaluronidase from bull testes is a fragment of the membrane‐bound PH‐20 enzyme

FEBS Letters

Kreil, Günther¹  Meyer, Michael F¹  Aschauer, Heinrich² 

[1] Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 11, A-5020 Salzburg, Austria;Sandoz Forschungsinstitut, Brunnerstrasse 59, A-1235 Vienna, Austria

关键词: Hyaluronidase;    PH-20;    Testes;    Fertilization;   

DOI  :  10.1016/S0014-5793(97)00936-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The membrane-bound PH-20 hyaluronidase is known to be essential for fertilization. Here we addressed the question whether the soluble hyaluronidase from bull teste is related to the PH-20 polypeptide. The sequence of the membrane-bound PH-20 hyaluronidase from bovine sperm was determined via cDNA cloning. In parallel, from a commercial preparation of bovine hyaluronidase the major 60-kDa form was purified to apparent homogeneity. The soluble enzyme was digested with two different proteases and with cyanogen bromide and the amino acid sequence of 44 different fragments was determined. All the peptide sequences could be aligned to the sequence deduced from the cloned cDNAs. Our results thus show that the soluble 60-kDa hyaluronidase from bovine testes is a glycoprotein derived from the sperm PH-20 enzyme. As compared to the primary translation product of the PH-20 mRNA, it lacks the signal peptide at the amino terminus and 56 amino acids at the carboxyl end. These results demonstrate that the soluble 60-kDa enzyme is a fragment of the PH-20 hyaluronidase. It is currently not known whether the soluble testes hyaluronidase has a distinct biological function.

【 授权许可】

Unknown