Isolation and characterization of glucocerebrosidase from human placental tissue
PG Pentchev, RO Brady, SR Hibbert, AE Gal… - Journal of Biological …, 1973 - ASBMB
Human placental glucocerebrosidase was purified 4000-fold to apparent homogeneity. The
most highly enriched preparation catalyzes the hydrolysis of 1 mmole of glucosylceramide
per mg of protein per hour. Although the molecular size of the enzyme depends on the
method of extraction, the purified protein is a tetramer composed of 4 catalytically active
units whose mass is 60,000 daltons each. The enzyme shows an absolute specificity for β-d-
glucopyranoside bonds and it is most active with the natural substrate glucocerebroside. It is …
most highly enriched preparation catalyzes the hydrolysis of 1 mmole of glucosylceramide
per mg of protein per hour. Although the molecular size of the enzyme depends on the
method of extraction, the purified protein is a tetramer composed of 4 catalytically active
units whose mass is 60,000 daltons each. The enzyme shows an absolute specificity for β-d-
glucopyranoside bonds and it is most active with the natural substrate glucocerebroside. It is …
