Human milk ribonuclease.
Two components having ribonuclease (EC 3.1.27.5) activity were isolated from human milk. Each component of human milk ribonuclease (RNAase) moved at a slightly different rate when electrophoresed on polyacrylamide gel but at the same rate when ultracentrifuged. The major component had a molecular weight of approx. 14 000, an isoelectric point of pH 7.9, and exhibited a broad absorbance maximum between 277 and 281 nm. Human milk RNAase hydrolyzed yeast RNA, poly(cytidylic acid) and poly(uridylic acid) but not DNA, poly(adenylic acid) or poly(guanylic acid). Maximum activity occurred at pH 7.7 and 60 degrees C. Amino acid analysis of the major component revealed a large number of alanine, valine, glycine and aspartic acids but no tryptophan or free sulfhydryl groups. Lysine was the N-terminal amino acid. Tryptic hydrolysis yielded 18 peptides, some of which are similar to those from bovine pancreatic RNAase. Human milk RNAase activity was increased in the presence of NaCl, KCl and sodium citrate and decreased by CaCl(2), MgCl(2), FeSO(4), ZnSO(4) and CuSO(4).
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D005260:Female; D006801:Humans; D008895:Milk, Human / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D012260:Ribonucleases / Q000378:metabolism*; D013379:Substrate Specificity; D014357:Trypsin / Q000494:pharmacology
D000596:Amino Acids; D010446:Peptide Fragments; D012260:Ribonucleases; D014357:Trypsin