Beta-glucuronidase of rat preputial gland. Crystallization, properties, carbohydrate composition, and subunits.
J Biochem
; 77(2): 427-38, 1975 Feb.
Article
em En
| MEDLINE
| ID: mdl-236293
ABSTRACT
Rat preputial gland beta-glucuronidase [ED 3.2.1.31] was purified by ammonium sulfate precipitation, ethanol fractionation, gel filtration on Sephadex G-200 and crystallization. The purified enzyme appeared homogeneous on electrophoresis in polyacrylamide gel, and on analytical ultracentrifugation and had a molecular weight of approximately 320,000, and a sedimentation coefficient of 12S. SDS polyacrylamide gel electrophoresis indicated that the enzyme consisted of subunits with molecular weight of 79,000, so the native enzyme appeared to be a tetramer. The Km with p-nitrophenyl beta-D-glucosiduronic acid as substrate was about 0.53 mM. The enzyme had a single pH optimum at 4.5. The enzyme had a very low content of sulphur-containing amino acid and contained 5.7 per cent carbohydrate, consisting of mannose, glucose, fucose, galactose, and glucosamine in a ratio of 44;9;6;2;41. Sialic acid was not detected in the crystallized enzyme.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Glândulas Sebáceas
/
Clitóris
/
Glucuronidase
Limite:
Animals
Idioma:
En
Ano de publicação:
1975
Tipo de documento:
Article