Document Detail


Characterization of adenohypophysial polypeptides by two-dimensional gel electrophoresis. II. Sulfated and glycosylated polypeptides.
MedLine Citation:
PMID:  7297761     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Adenohypophysial sulfated and glycosylated polypeptides were studied by high-resolution two-dimensional polyacrylamide-gel electrophoresis followed by fluorography. The preparations analyzed were the following: (a) homogenates from cow and rat anterior pituitary slices labeled in vitro either with [35S]sulfate or D-[6-3H]glucosamine; (b) materials released from bovine adenohypophysis slices pulse labeled with [35S]sulfate; and (c) purified fractions of bovine prolactin granules stripped by detergent treatment of their limiting membrane. A heterogeneous family of sulfated components, almost all glycosylated, differing in their peptide moieties as well as in their isoelectric points, was revealed in the glandular tissue. The major of these components (apparent Mr approximately 70 000; pI approximately 4.8), which was also highly labeled by L-[3H]-leucine (Zanini, A., and Rosa, P. (1981) Mol. Cell. Endocrinol. 24), might be a secretory protein because it accumulates in the medium during chase incubation of bovine pituitary slices in vitro. This sulfated component, which was more concentrated in the bovine than in the rat gland, was present in purified bovine prolactin granules stripped of their limiting membrane. However, the available evidence suggests that this might not be the only subcellular location of the sulfated polypeptide in the pituitary tissue.
Authors:
P Rosa; A Zanini
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Molecular and cellular endocrinology     Volume:  24     ISSN:  0303-7207     ISO Abbreviation:  Mol. Cell. Endocrinol.     Publication Date:  1981 Nov 
Date Detail:
Created Date:  1982-01-20     Completed Date:  1982-01-20     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  7500844     Medline TA:  Mol Cell Endocrinol     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  181-93     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Cattle
Electrophoresis, Polyacrylamide Gel
Female
Fetus / analysis
Glucosamine / metabolism*
Molecular Weight
Peptides / analysis*,  metabolism
Pituitary Gland, Anterior / analysis*
Pregnancy
Rats
Sulfates / metabolism*
Chemical
Reg. No./Substance:
0/Peptides; 0/Sulfates; 3416-24-8/Glucosamine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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