Isolation and Amino Acid Sequences of Proline-rich Peptides of Human Whole Saliva
- 30 June 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 86 (1) , 79-86
- https://doi.org/10.1093/oxfordjournals.jbchem.a132522
Abstract
Three basic peptides with extremely high proline contents were isolated from human whole saliva. The amino acid sequences of two of these proline-rich peptides comprising 57 and 38 residues were determined by conventional methods. The sequence suggested that the smaller peptide was derived from the larger one and also revealed the occurrence of characteristic repeating units within the molecules. The present study is the first to describe this structural feature of proline-rich proteins or peptides.This publication has 5 references indexed in Scilit:
- A technique for the removal of pyroglutamic acid from the amino terminus of proteins using calf liver pyroglutamate amino peptidaseBiochemical and Biophysical Research Communications, 1978
- Amino Acid Sequences of Fragments I and II Obtained by Cyanogen Bromide Cleavage of Rat Serum Albumin1The Journal of Biochemistry, 1978
- Chemical and physical characterization of a phosphoprotein, Protein C, from human saliva and comparison with a related protein ABiochemical Journal, 1977
- Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva.Journal of Biological Chemistry, 1977
- The isolation of some basic proline-rich proteins from human parotid salivaArchives of Oral Biology, 1977