Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Arylsulfatase A was extracted and purified from boar epididymal sperm acrosomes. Acrosomes were extracted by sonication in 50 mM Tris-maleate buffer containing 50 mM MgCl2, pH 6.1, followed by treatment with 50 mM Tris-maleate plus 0.2% Brij-35, pH 6.1. Purification of arylsulfatase A was performed with a three-step procedure consisting of centrifugation (85,000 X g), affinity chromatography with p-aminobenzamidine-Sepharose followed by chromatography on diethyaminoethyl (DEAE) Sephadex. The specific activity of the purified enzyme was 54 mumol/h per mg protein. The purified arylsulfatase did not contain any detectable acrosin or hyaluronidase activities. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis revealed a major band with an estimated molecular weight of 65,000 daltons. Properties of arylsulfatase A, determined by hydrolysis of p-nitrocatechol sulfate, indicated that the enzyme was inhibited 46% by 3.1 microM Ag+ and had a pH optimum of 4.2. Boar acrosomal arylsulfatase A dispersed the cumulus cells of ovulated hamster and rabbit eggs as well as those of follicular pig eggs. No effect of the enzyme on the zona pellucida or the oolemma was observed.
 ...
PMID:Purification of boar acrosomal arylsulfatase A and possible role in the penetration of cumulus cells. 614 55

Carbohydrate residues on membrane proteins from sperm are important in gamete interaction. In recent years, Arylsulfatase A (AS-A) has been acquiring an important role from the various putative gamete interaction responsibles in sperm. The aim of this study was to determine if the capacitated boar sperm Arylsulfatase-A (AS-A), contains D-mannose, N-acetylglucosamine and/or sialic acid residues by its purification using affinity chromatography with Concanavalia ensiformis Agglutinin(Con-A) or Wheat Germ Agglutinin (WGA) as ligands. Sperm samples were capacitated in TALP-HEPES medium. Protein extract was added to the affinity columns. Sequencing of retained proteins was done after SDS-PAGE. Total capacitated sperm proteins electrophoresis showed molecular masses between 14 kDa and 102 kDa. A major band of 68 kDa, and 2 minor bands of 52 kDa and 47 kDa were observed. They were AS-A, hyaluronidase and lactadherin, respectively. The Con-A-retained proteins (RP) pattern showed bands from 14 to 98 kDa. After sequencing and BLAST analysis, the 62 kDa band corresponded to Arylsulfatase-A. The WGA RP fraction showed bands from 14 to 100 kDa. The 65 kDa band corresponded to AS-A. This study showed that AS-A has mannose, N-acetylglucosamine and/or sialic acid residues as part of its glycosilation. In this study AS-A was isolated from boar capacitated sperm by affinity chromatography using separately Con-A and WGA, indicating that there are mannose, N-acetylglucosamine and/or sialic acid residues in its glycosilation. AS-A is a membrane protein of capacitated sperm. Further investigation is needed to fully characterize the glycosidic residues bore by AS-A and to determine its function.
 ...
PMID:Carbohydrate affinity chromatography indicates that arylsulfatase-A from capacitated boar sperm has mannose and N-acetylglucosamine/sialic acid residues. 1705 Mar 27