Primary Structure of a Non-Secretory Ribonuclease from Bovine Kidney

• Published in: Journal of biochemistry (Tokyo) Vol. 104; no. 2; pp. 289 - 296
• Main Authors: Irie, Masachika, Nitta, Reiko, Ohgi, Kazuko, Niwata, Yasushi, Watanabe, Hideaki, Iwama, Masanori, Beintema, Jaap J., Sanda, Akihiro, Takizawa, Yoshio
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 01.08.1988
• Subjects: Amino Acid Sequence; Amino Acids - analysis; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Cattle; Chromatography, High Pressure Liquid; Chymotrypsin - metabolism; Cyanogen Bromide; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Humans; Hydrolases; Kidney - enzymology; Molecular Sequence Data; non-secretory ribonuclease; Oxidation-Reduction; Pancreas - enzymology; Ribonucleases; Staphylococcus aureus - enzymology; Terminology as Topic; Trypsin - metabolism; Tryptophan - analysis; Vertebrata; Mammalia; Bovine; Active site; Primary structure; Artiodactyla; Ribonuclease; Ungulata; Kidney
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a122460

The primary structure of a non-secretory ribonuclease from bovine kidney (RNase K2 was determined. The sequence determined was VPKGLTKARWFEIQHIQPRLLQCNKAMSGVNNYTQHCKPENTFLIINVFQDVTAVCDMPNIICKNGRHNCHQSPKPVNLTQCNFIAGRYPDCRYHDDAQYKFFIVACDPPQKTDPPYHLVPVHLDKYF. The sequence homology with human non-secretory RNase, bovine pancreatic RNase, and human secretory RNase are 46, 34.6, and 32.3%, respectively. The bovine kidney RNase has two inserted sequences, a tripeptide at the N-terminus and a heptapeptide between the 113th and 114th position of bovine pacreatic RNase; on the other hand, it is deleted of the hexapeptide consisting of the 17th to the 22nd amino acid residue of RNase A. The amino acid residues assumed to be the constituents of the bovine pancreatic RNase active site are all conserved except F120 (L in RNase K2).