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- W1977278634 abstract "Abstract 1. Synthesis of α-lactalbumin and β-lactoglobulin has been carried out in vitro by cell-free systems consisting of microsomes or bound polyribosomes derived from the mammary gland of the lactating ewe. 2. The two proteins labelled with 14C and synthesized in vitro have been identified by; (a) their behaviour on chromatography with CM-cellulose and Sephadex G-100 columns and on electrophoresis in polyacrylamide gel: (b) their antigenic properties: (c) their molecular weights, determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate; (d) the number of peptides produced by tryptic hydrolysis of β-[14C]lactoglobulin and their chromatographic and electrophoretic properties. 3. The distribution of the radioactivity between the peptides resulting from tryptic hydrolysis of β-lactoglobulin and the determination of the radioactivity of the N-terminal amino acid suggest that most of the radioactive amino acids incorporated in vitro into β-lactoglobulin correspond to the completion of peptide chains which began in vivo." @default.
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- W1977278634 date "1972-03-01" @default.
- W1977278634 modified "2023-10-14" @default.
- W1977278634 title "In vitro synthesis of α-lactalbumin and β-lactoglobulin by microsomes and bound polyribosomes from the mammary gland of lactating sheep" @default.
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- W1977278634 doi "https://doi.org/10.1016/0005-2787(72)90275-4" @default.
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