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HUMAN SPERM β‐GLUCURONIDASE IS POORLY EXTRACTABLE BY TRITON X‐100
Author(s) -
BRANDELLI ADRIANO,
MIRANDA PATRICIA V.,
TEZÓN JORGE G.
Publication year - 1996
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1996.0040
Subject(s) - glucuronidase , chaotropic agent , glycoside hydrolase , sperm , chemistry , colchicine , enzyme , fraction (chemistry) , biochemistry , solubilization , chromatography , biology , botany , genetics
A part of sperm glycosidase activities was detected as detergent‐insoluble after sequential extractions with Triton X‐100. Sixty per cent of total β‐glucuronidase activity was found in the detergent‐insoluble fraction. This portion of β‐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 β‐glucuronidase is tightly associated to the Triton X‐100 resistant fraction.