Linked Life Data

7118851

Source:http://linkedlifedata.com/resource/pubmed/id/7118851

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1982-12-2
pubmed:abstractText
The enzyme mutarotase [aldose 1-epimerase, EC 5.1.3.3] from hog kidney cortex was separated into four fractions (designated types I, II, III, and IV in order of elution) by column chromatography on DEAE-cellulose. Two major forms, types I and II, were purified to homogeneity as judged by polyacrylamide gel electrophoresis and isoelectric focusing on thin layer polyacrylamide gel. Types I, II, III, and IV had isoelectric points of 5.78, 5.48, 5.23, and 5.10, respectively. The following physicochemical properties were common to all four types: molecular weight, 41,000; Km for alpha-D-glucose at pH 7.4 and 25 degrees C, 19 mM; optimum pH, 6.5-7.5; optimum temperature, 30-37 degrees C; heat stability, up to 50 degrees C. On double immunodiffusion, the four types of mutarotase gave single precipitin lines, which fused completely with each other, against the antibody to purified type II enzyme. Types I and II had an identical amino-terminal residue, arginine, and an identical carboxyl-terminal sequence, -(Phe-Phe-Ser-Val)-Val-Ala. The amino acid composition of type I was almost identical with that of type II. Very similar tryptic peptide maps were obtained from types I and II, with only a few points of variance. These results suggest that the four types of hog kidney mutarotase are quite similar but not identical.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1889-98
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Purification and characterization of multiple forms of mutarotase from hog kidney cortex.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't