Bovine liver .BETA.-acetylhexosaminidase. Purification by hydrophobic affinity chromatography and heterogeneity.
- 31 December 1977
- journal article
- research article
- Published by Pharmaceutical Society of Japan in CHEMICAL & PHARMACEUTICAL BULLETIN
- Vol. 26 (10) , 3225-3228
- https://doi.org/10.1248/cpb.26.3225
Abstract
Bovine liver .beta.-acetylhexosaminidase A (Hex A) and B (Hex B) were purified by hydrophobic affinity chromatography. Octyl Sepharose CL-4B was more effective than phenyl sepharose CL-4B as an adsorbent. Both the crude and the purified preparations of Hex A and Hex B exhibited extensive heterogeneity when focused on a polyacrylamide gel plate with pH gradient; Hex A gave at least 20 bands with pI''s [isoelectric points] ranging from 5.0-7.0, and Hex B at least 14 bands with PI''s ranging from 6.5-8.5. Stepwise elution with increasing pH from a CM[carboxymethyl]-cellulose column resulted in rough separation of Hex A and Hex B into overlapping classes.This publication has 6 references indexed in Scilit:
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