VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Isolation, purification and properties of a carboxypeptidase inhibitor from human blood serum

   
Trapeznikova S.S., Mardashev S.R.
PubMed Id: 1216761
Year: 1975  Volume: 21  Issue: 4  Pages: 417-422
Partially purified low molecular component, which inhibited the carboxypeptidase N activity in samples with hippuryl-L-lysine and bradikinine as substrates, was isolated from human blood serum by means of chromatography on DEAE-Sephadex, ultrafiltration of the fractions obtained through Amicon membranes UM-10 or UM-2 and subsequent gel filtration through Sephadex G-10. The probable molecular weight of the inhibitor was 2000. The inhibitor was thermolabile; its inhibitory activity was decreased by 50% after 30 min boiling in 0.01 M phosphate buffer, pH 7.8. Trypsin and chymotrypsin did not influence the inhibitory properties of the factor. Hydrolysis of the low molecular component in 6 N HCl at 110 degrees C within 18 hrs and subsequent studies of the amino acid composition showed a number of amino acids in the hydrolysate; the hydrolysate exhibited the inhibitor activity of the initial substance.
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Trapeznikova, S. S., Mardashev, S. R. (1975). Isolation, purification and properties of a carboxypeptidase inhibitor from human blood serum. Voprosy Meditsinskoi Khimii, 21(4), 417-422.
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