Purification of hyaluronidase from human placenta.
J Biochem, 1977/2;81(2):485-94.
Yamada M, Hasegawa E, Kanamori M
PMID: 14951
Impact factor: 3.241
Abstract
Hyaluronidase [EC 3.2.1.35] was isolated from human placenta and purified by ammonium sulfate fractionation, DEAE-cellulose column chromatography and gel filtration on Sephadex G-150. Its isoelectric point was at pH 5.2 and the molecular weight was 7 X 10(4) based on Sephadex G-200 gel filtration data. This enzyme was very stable at temperatures below 30 degree, but was almost completely inactivated at 60degree within 30 min. Its optimum pH was 3.9, a characteristic property of a lysosomal hyaluronidase. The Michaelis constant was 1.18 x 10(-1) mg per ml with purified hyaluronate. This enzyme depolymerized hyaluronate, chondroitin, chondroitin 4-sulfate and 6-sulfate, and the end product formed from hyaluronate was tetrasaccharide. Its biological diffusing activity was statistically significant on intracutaneous injection of 1.86 mU of the hyaluronidase into the back skine of a rabbit.
MeSH terms
Animals; Chondroitin; Chondroitin Sulfates; Dermatan Sulfate; Female; Humans; Hyaluronic Acid; Hyaluronoglucosaminidase; Hydrogen-Ion Concentration; Kinetics; Mice; Molecular Weight; Placenta; Rabbits; Temperature
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