pH-dependent association-dissociation of GM1-.BETA.-galactosidase purified from porcine spleen.

J-STAGE

この論文をさがす

説明

A β-galactosidase [EC 3. 1. 23] catalyzing the hydrolysis of GM1-ganglioside was purified from porcine spleen to a homogeneous form. By applying a hydrophobic chromatography procedure as the first purification step, the enzyme could be purified through subsequent purification steps as a dissociated form. The purified enzyme was a monomer with an apparent molecular weight of 70, 000-74, 000 at neutral pH and associated to a dimer with an apparent molecular weight of 158, 000-160, 000 at acidic pH, near optimal for its activity (pH 4.6). It had specific activities of 1, 820μmol/mg/h towards GM1 with an apparent Km of 3.18×10-5M, 1, 880μmol/mg/h towards lactosylceramide with an apparent Km of 1.99×10-4M, and 1, 340μmo1/mg/h towards p-nitrophenyl-β-galactopyranoside (pNp-β-galactoside) with an apparent Km of 2.14×10-4M. Kinetic studies suggested that common catalytic site (s) cleaved the two natural substrates mentioned above.

収録刊行物

詳細情報 詳細情報について

問題の指摘

ページトップへ