Results 171 to 180 of about 114,651,738 (212)
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On the activation of pepsinogen

Biochemical and Biophysical Research Communications, 1971
Abstract The content of carbohydrates in chromatographically pure swine pepsin and pepsinogen is shown to be negligible. Therefore the scission of carbohydrate moiety cannot trigger the activation of pepsinogen. Thermolysin at pH 5 converts swine pepsinogen into a mixture of pepsin and leucyl-pepsin which emphasizes the decisive role of limited ...
V M, Stepanov   +5 more
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Amphibian Pepsinogens: Purification and Characterization of Xenopus Pepsinogens, and Molecular Cloning of Xenopus and Bullfrog Pepsinogens

Journal of Biochemistry, 2001
Two pepsinogens (Pg C and Pg A) were isolated from the stomach of adult Xenopus laevis by Q-Sepharose, Sephadex G-75, and Mono-Q column chromatographies. Autolytic conversion and activation of the purified Pgs into the pepsins were examined by acid treatment.
M, Ikuzawa   +3 more
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Influence of pepsinogen gene polymorphisms on serum pepsinogen

Annals of Human Genetics, 1997
We identified pepsinogen C (PGC) gene polymorphisms by means of PCR, which amplified DNA in the region within the intron between exons 7 and 8, and by 6% polyacrylamide gel electrophoresis. Six alleles were found in a Japanese population. The frequencies of these alleles in 408 unrelated Japanese individuals were 0.074, 0.026, 0.335, 0.237, 0.016 and 0.
Z, Yamagata   +6 more
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The Ratio of Pepsinogen A to Pepsinogen C: A Sensitive Test for Atrophic Gastritis

Scandinavian Journal of Gastroenterology, 1989
To diagnose fundic atrophic (type A) gastritis as part of the clinical investigation of various diseases or for epidemiologic purposes, a simple and reliable diagnostic test would be of great value. We studied circulating levels of pepsinogen A (PGA) and pepsinogen C (PGC) in 179 patients with fundic atrophic gastritis, 29 unselected patients with ...
K Borch
exaly   +3 more sources

Pepsinogens in Health and Disease

Critical Reviews in Clinical Laboratory Sciences, 1993
Pepsinogens, precursors of pepsins (potent and abundant digestive enzymes that are the primary products of the gastric chief cells), are members of the family of aspartic proteases. Because of the heterogeneity of pepsinogens, several classifications have appeared in the literature.
M. Plebani, Or. Sander Szabo
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Pepsinogen

Nihon rinsho. Japanese journal of clinical medicine, 1995
It is generally accepted that extensive chronic atrophic gastritis is a precursor to gastric cancer in populations at high risk for this tumor. To improve the effectiveness of gastric cancer screening, we have devised a new screening method that investigates the serum pepsinogen levels and applied a serum pepsinogen test to mass screening for gastric ...
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Genetics of pepsinogen I

Annals of Human Genetics, 1980
A study of 948 Norwegians including 118 matings with 429 children provided evidence that the Pg I group of pepsinogens must be coded for by more than one gene locus. At the Pg5 locus the alleles Pg5N, Pg5F and Pg5S with frequencies 0.644, 0.059 and 0.004, each code for a single electrophoretic isozyme band responsible for Pg phenotypes Pg 5, intense Pg
L, Korsnes, T, Gedde-Dahl
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Pepsinogens in gastric carcinomas

Human Pathology, 1986
Polyclonal rabbit antisera raised against the two major groups of human pepsinogens (PG I and PG II) were used in an immunohistochemical study of human gastric carcinomas. Thirty-two carcinomas, classified histologically according to the Lauren classification as diffuse or intestinal, were studied; and the staining patterns of the tumor and adjacent ...
R M, Busby-Earle   +2 more
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Pepsinogen

Journal of Clinical Gastroenterology, 1987
Pepsin is a potent proteolytic enzyme stored and secreted by chief cells in an inactive precursor form, pepsinogen. Its secretion is modulated by both cAMP and calcium-dependent mechanisms. Abnormalities in levels of pepsinogen and its various isozymogens have been linked clinically, epidemiologically, and experimentally to peptic ulcer disease and ...
M D, Basson, I M, Modlin
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THE CONTROL OF PEPSINOGEN SECRETION*

Annals of the New York Academy of Sciences, 1967
SummaryThe peptic cell makes and secretes a protein (pepsinogen) and the cellular mechanisms governing the rate of synthesis and its relation to secretion are described and schematically illustrated.The peptic cell as a system secreting protein exists side by side with the parietal cell transporting H+, Cl, water and electrolytes.
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