The role of covalently bound fatty acids in the degradation of human gastric mucus glycoprotein

Amalia Slomiany, Zofia Jozwiak, Atsushi Takagi, Bronislaw L. Slomiany

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67 Scopus citations


The undegraded high-molecular-weight glycoprotein of human gastric mucus has been isolated free of noncovalently bound proteins and lipids, as judged by gel filtration, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, cesium chloride density gradient centrifugation, and lipid analysis. Mild alkaline methanolysis of the thoroughly delipidated glycoprotein revealed that, on the average, the native undegraded glycoprotein contains 2.9 mol of acyl linked fatty acids/mg glycoprotein. The low-molecular-weight glycoprotein subunits, obtained after pepsin digestion, contain 2 nmol of acyl linked fatty acids/mg glycopeptide. The highest content of covalently bound fatty acids was found in the fraction of glycoprotein which remained undegraded after pepsin digestion. On the average, 10.2 mol of fatty acids/mg was substituted on this pepsin-resistant glycoprotein. After deacylation with hydroxylamine, the undegraded pepsinresistant glycoprotein became susceptible to proteolytic cleavage. The obtained results suggest that fatty acids covalently bound to gastric mucus glycoprotein are involved in the regulation of proteolytic digestion of mucus glycoprotein in the stomach.

Original languageEnglish (US)
Pages (from-to)560-567
Number of pages8
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - Mar 1984
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology


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