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PMID: 540000 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Human salivary proline-rich (Pr) proteins: a posttranslational derivation of the phenotypes.

Biochemical genetics ·Vol. 17 ·No. 11-12 ·1979-12-00 ·Pages 1061-77

Karn RC, Friedman RD, Merritt AD

Abstract

The acidic proline-rich proteins (Pr) showing genetic polymorphism were purified from human parotid salivas by gel filtration and ion exchange chromatography. Molecular weight determinations, amino acid composition analyses, and polypeptide mapping experiments indicate that the Pr 3 protein is a fragment of the Pr 1 protein. Studies of a parotid saliva factor capable of converting Pr 1 to Pr 3 and Pr 2 to Pr 4 indicate that Pr 3 and Pr 4 are generated from Pr 1 and Pr 2, respectively. Evidence suggests that the converting factor is a protease capable of posttranslationally cleaving Pr 1 and Pr 2, the primary or derived products of alleles Pr1 and Pr2.

MeSH Terms
Amino Acids/analysis Humans Molecular Weight Parotid Gland/metabolism Polymorphism, Genetic Proline/genetics Proteins/analysis,genetics,isolation & purification Saliva/metabolism
Chemicals
Amino Acids Proteins Proline
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Karn R C
Friedman R D
Merritt A D
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26 references, click to expand
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Article Info
Journal
Biochemical genetics
Abbr.
Biochem Genet
ISSN
0006-2928
DOI
10.1007/BF00504345
Published
1979-12-00
Pages
1061-77
Language
English
Region
United States
NLM ID
0126611
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00504345 View journal details
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