Literature DB >> 6696901

Identification of the proteins exposed on the cytoplasmic surface of the pancreatic zymogen granule.

D LeBel, M Beattie.   

Abstract

Lactoperoxidase-catalyzed 125I-iodination was used to label pancreatic zymogen granules. Membrane proteins facing the cytoplasmic surface were specifically labeled. Two low molecular weight proteins of 17 000 and 15 000 were intensely labeled at 0 degree C. Another small 13 kDa protein was strongly iodinated at 25 degrees C along with some others, including the 29 kDa subunit of the ATP diphosphohydrolase. The major glycoprotein of the granule membrane was not iodinated but the presence of an iodinated 80 kDa protein suggests that proteolytic fragments of the 92 kDa glycoprotein were accessible to iodination on the intact granule. These proteins localized on the cytoplasmic surface of the granule are believed to play a major role in the exocytotic phenomenon of the exocrine pancreas.

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Year:  1984        PMID: 6696901     DOI: 10.1016/0005-2736(84)90061-0

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  A single gene encodes membrane-bound and free forms of GP-2, the major glycoprotein in pancreatic secretory (zymogen) granule membranes.

Authors:  S Fukuoka; S D Freedman; G A Scheele
Journal:  Proc Natl Acad Sci U S A       Date:  1991-04-01       Impact factor: 11.205

2.  Purification and characterization of the apical plasma membrane of the rat pancreatic acinar cell.

Authors:  E Paul; Y Hurtubise; D LeBel
Journal:  J Membr Biol       Date:  1992-04       Impact factor: 1.843

  2 in total

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