Mutarotase in erythrocytes: isolation and properties.

Science (New York, N.Y.) ·Vol. 158 ·No. 3800 ·1967-10-27 ·Pages 498-9

Sacks W

Abstract

Mutarotase was found in lysed human erythrocytes and in hemoglobin. The enzyme was partially purified by treatment with ethanol and chloroform at -15 degrees C. It was nondialyzable and heat sensitive, and was inhibited by D-galactose, L-arabinose, D-ribose, D-xylose, and D-arabinose.

MeSH Terms

Arabinose Chemical Phenomena Chemistry, Physical Chloroform Edetic Acid Erythrocytes/enzymology Ethanol Galactose Hemoglobins Humans Isomerases/antagonists & inhibitors,blood Kinetics Ribose Xylose

Chemicals

Hemoglobins Ethanol Ribose Chloroform Edetic Acid Xylose Arabinose Isomerases Galactose

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Sacks W

Article Info

Journal

Science (New York, N.Y.)

Abbr.

Science

ISSN

0036-8075

DOI

10.1126/science.158.3800.498

Published

1967-10-27

Pages

498-9

Language

English

Region

United States

NLM ID

0404511

Subset

External Links

PubMed source DOI: 10.1126/science.158.3800.498 View journal details

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