| Literature DB >> 7357015 |
A Amemura, Y Konishi, T Harada.
Abstract
Crystalline isoamylase of Pseudomonas amyloderamosa was found to be contaminated with a trace of proteolytic enzyme. This contaminant digested the isoamylase under neutral or alkaline conditions, especially in the presence of sodium dodecyl sulfate (SDS). A reliable molecular weight of the enzyme was obtained by SDS-polyacrylamide gel electrophoresis and by gel filtration on Sepharose-6B in 6 M guanidine-hydrochloride after heat inactivation of the contaminant. The molecular weight of the undergraded polypeptide chain of the isoamylase was about 90 000. The lower molecular weight and the subunit structure of the enzyme reported previously are incorrect.Entities:
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Year: 1980 PMID: 7357015 DOI: 10.1016/0005-2744(80)90077-7
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002