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Purification of a novel apolipoprotein H-like milk protein with ribonucleolytic and cell-free translation inhibitory activities

Authors
Journal
Life Sciences
0024-3205
Publisher
Elsevier
Publication Date
Volume
67
Issue
8
Identifiers
DOI: 10.1016/s0024-3205(00)00683-4
Keywords
  • Bovine Milk
  • Ribonuclease
  • Apolipoprotein H
Disciplines
  • Biology
  • Design

Abstract

Abstract A new whey protein designated apolipoprotein H-like whey protein, with a molecular weight of 62 kDa and an N-terminal amino acid sequence similar to that of apolipoprotein H, was isolated from bovine milk. The isolation procedure involved removal of globulin from acid whey by precipitation with 1.8M (NH 4) 2SO 4, followed by addition of (NH 4) 2SO 4 to attain a concentration of 3.6M. Subsequent steps included chromatography on CM-Sepharose and Mono S and elution of the adsorbed protein of interest with a linear NaCl gradient. The new whey protein displayed some ribonuclease (RNase) activity. It was most active at pH 7.5 with yeast transfer RNA (tRNA) as substrate and showed potent specific ribonucleolytic activity toward poly C. It inhibited cell-free translation in a rabbit reticulocyte lysate system with an IC 50 of approximately 63 nM.

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