Open AccessGuinea‐Pig Pancreatic Ribonucleases
Author(s) -
BERG Annelies,
HENDETIMMER Lies,
HOFSTEENGE Jan,
GAASTRA Wim,
BEINTEMA Jaap J.
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11507.x
Subject(s) - ribonuclease , biochemistry , s tag , pancreatic ribonuclease , bovine pancreatic ribonuclease , ribonuclease iii , guinea pig , protein primary structure , biology , asparagine , leucine , peptide sequence , chemistry , amino acid , rna , rna interference , gene , endocrinology
Two ribonucleases were isolated from guinea‐pig pancreas by extraction with 0.125 M sulfuric acid, precipitation with acetone and chromatography on carboxymethyl‐cellulose. The amino acid sequences were determined from tryptic digests of the aminoethylated proteins. The tryptic peptides were positioned in the sequence by homology with other pancreatic ribonucleases. Both ribonucleases not only differ in the presence (ribonuclease B) or absence of carbohydrate (ribonuclease A), but also at 31 positions of the amino acid sequence. In guinea‐pig ribonuclease B a leucine/proline heterogeneity was found at position 64. The carbohydrate in guinea‐pig ribonuclease B is attached to asparagine residues at positions 21 and 34. The carbohydrate‐free guinea‐pig ribonuclease A possesses a recognition site for sugar attachment in the sequence Asn‐Val‐Ser (62–64).