Primary structure of a non-secretory ribonuclease from bovine kidney.
The primary structure of a non-secretory ribonuclease from bovine kidney (RNase K2) was determined. The sequence determined was VPKGLTKARWFEIQHIQPRLLQCNKAMSGV NNYTQHCKPENTFLHNVFQDVTAVCDMPNIICKNGRHNCHQSPKPVNLTQCNFIAGRYPDC RYHDDAQYKFFIVACDPPQKTDPPYHLVPVHLDKYF. 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 pancreatic 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).
Irie
M
M
Department of Microbiology, Hoshi College of Pharmacy, Tokyo.
Nitta
R
R
Ohgi
K
K
Niwata
Y
Y
Watanabe
H
H
Iwama
M
M
Beintema
J J
JJ
Sanda
A
A
Takizawa
Y
Y
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism; D003488:Cyanogen Bromide; D006801:Humans; D007668:Kidney / Q000201:enzymology*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010179:Pancreas / Q000201:enzymology; D012260:Ribonucleases; D013211:Staphylococcus aureus / Q000201:enzymology; D009626:Terminology as Topic; D014357:Trypsin / Q000378:metabolism; D014364:Tryptophan / Q000032:analysis
D000596:Amino Acids; D014364:Tryptophan; D012260:Ribonucleases; D002918:Chymotrypsin; D014357:Trypsin; D003488:Cyanogen Bromide