Human sperm beta-glucuronidase is poorly extractable by Triton X-100.
A part of sperm glycosidase activities was detected as detergent-insoluble after sequential extractions with Triton X-100. Sixty per cent of total beta-glucuronidase activity was found in the detergent-insoluble fraction. This portion of beta-glucuronidase was resistant to extractions in the presence of 1 M KCl, chaotropic agents, colchicine or cytochalasine B, being only partially solubilized by 3 M KCl or DNAse I treatment. Results demonstrate that beta-glucuronidase is tightly associated to the Triton X-100 resistant fraction.
Brandelli
A
A
Departamento de Bioquimica, Instituto de Biociências, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brasil.
Miranda
P V
PV
Tezón
J G
JG
D000199:Actins / Q000737:chemistry / Q000187:drug effects; D002458:Cell Fractionation; D003598:Cytoskeletal Proteins / Q000187:drug effects / Q000302:isolation & purification; D003850:Deoxyribonuclease I / Q000494:pharmacology; D005966:Glucuronidase / Q000737:chemistry* / Q000302:isolation & purification*; D006801:Humans; D008297:Male; D017830:Octoxynol / Q000737:chemistry* / Q000494:pharmacology; D011108:Polymers; D012995:Solubility; D013094:Spermatozoa / Q000201:enzymology*
D000199:Actins; D003598:Cytoskeletal Proteins; D011108:Polymers; D017830:Octoxynol; D003850:Deoxyribonuclease I; D005966:Glucuronidase