PMID: 6971128Feb 27, 1981Paper

The interaction of alpha 1-antitrypsin with trypsin, chymotrypsin and human leukocyte elastase as revealed by end group analysis

Biochimica Et Biophysica Acta
R R Martodam, I E Liener

Abstract

Complexes of alpha 1-antitrypsin with trypsin, alpha-chymotrypsin, and human leukocyte elastase were purified and examined for amino-terminal sequences. These complexes were shown to possess the expected N-terminal sequences for alpha 1-antitrypsin and the corresponding enzymes; no newly generated amino groups could be detected. Each of these three complexes was dissociated at pH 10, and the inhibitor component was isolated. When the latter was subjected to sodium dodecyl sulfate gel electrophoresis a single band was obtained in all cases, and its molecular weight was judged to be 45 000 compared to 52 000 for alpha 1-antitrypsin. Examination of the N-terminal sequence of these modified inhibitors, however, disclosed the presence of two molecular species with different N-termini. The predominant species had the N-terminal sequence previously reported for post-complex alpha 1-antitrypsin (Johnson, D. and Travis, J. (1978) J. Biol. Chem. 253, 7142-7144) and the same carboxyl sequence as alpha 1-antitrypsin. Present in lesser amounts was a species which had retained the same N-terminal sequence as alpha 1-antitrypsin, but of which the C-terminus was resistant to the action of carboxypeptidases A and B. From these results it is con...Continue Reading

References

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Citations

Jan 1, 1985·The International Journal of Biochemistry·S D Pearson, J C Gan
Dec 7, 1981·FEBS Letters·R W CarrellD R Boswell
Jul 22, 1982·Nature·R W CarrellD R Boswell
Sep 26, 2012·The FEBS Journal·Christian E H SchmelzerAndrea Heinz
Feb 21, 2021·Journal of Crohn's & Colitis·Núria Solà TapiasFrédérick Barreau
Apr 28, 1983·Biochimica Et Biophysica Acta·D R BoswellR W Carrell

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