Digestion

Original Paper

Identification of Mucus Glycoprotein Fatty Acyltransferase Activity in Human Gastric Mucosa

Liau Y.H. · Slomiany B.L. · Slomiany A. · Piasek A. · Palmer D. · Rosenthal W.S.

Author affiliations

Gastroenterology Research Laboratory and Sarah C. Upham Section of Gastroenterology, Department of Medicine, New York Medical College, Research Center, Metropolitan Hospital, New York, NY., USA

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Digestion 1985;32:57–62

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: October 09, 1984
Accepted: December 17, 1984
Published online: January 29, 2009
Issue release date: 1985

Number of Print Pages: 6
Number of Figures: 0
Number of Tables: 0

ISSN: 0012-2823 (Print)
eISSN: 1421-9867 (Online)

For additional information: https://www.karger.com/DIG

Abstract

The enzymatic activity which catalyzes the transfer of palmitic acid from palmitoyl coenzyme A to gastric mucus glycoprotein was demonstrated in antral and fundic mucosa of normal human stomach. Subcellular fractionation studies revealed that with both types of mucosa the enzyme activity was present in the microsomal fraction. The antral and fundic mucosa also exhibited similar enzyme activities, showed identical pH optimum, and required detergent, NaF and dithiothreitol. Optimum enzymatic activity for fatty acylation of mucus glycoprotein was obtained with 0.5% Triton X-100, 25 mM NaF, and 25 mM dithiothreitol at a pH of 7.4. The 14C-labeled product of the reaction comigrated on CsCl density gradient centrifugation with gastric mucus glycoprotein and contained the ester-bound palmitic acid.

© 1985 S. Karger AG, Basel




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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: October 09, 1984
Accepted: December 17, 1984
Published online: January 29, 2009
Issue release date: 1985

Number of Print Pages: 6
Number of Figures: 0
Number of Tables: 0

ISSN: 0012-2823 (Print)
eISSN: 1421-9867 (Online)

For additional information: https://www.karger.com/DIG


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