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Open AccessJournal ArticleDOI

The oxidative inactivation of human alpha-1-proteinase inhibitor. Further evidence for methionine at the reactive center.

David A. Johnson, +1 more
- 25 May 1979 - 
- Vol. 254, Iss: 10, pp 4022-4026
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This article is published in Journal of Biological Chemistry.The article was published on 1979-05-25 and is currently open access. It has received 467 citations till now. The article focuses on the topics: Reactive center & Methionine.

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Production of Large Amounts of Hydrogen Peroxide by Human Tumor Cells

TL;DR: Constitutive generation of large amounts of reactive oxygen intermediates, if it occurs in vivo, might contribute to the ability of some tumors to mutate, inhibit antiproteases, injure local tissues, and therefore promote tumor heterogeneity, invasion, and metastasis.
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Neutrophil Function: From Mechanisms to Disease

TL;DR: A survey of basic neutrophil biology, with an emphasis on examples that highlight the function of neutrophils not only as professional killers, but also as instructors of the immune system in the context of infection and inflammatory disease.
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Persistent oxidative stress in cancer

TL;DR: It is suggested that the concept of ‘persistent oxidative stress in cancer’ may open up a new research area, explaining part of the characteristic tumor biology of cancer such as activated transcription factors and proto‐oncogenes, genomic instability, chemotherapy‐resistance, invasion and metastasis.
References
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Journal ArticleDOI

A spectrophotometric determination of trypsin and chymotrypsin

TL;DR: A sensitive spectrophotometric assay for trypsin and chymotrypsin using synthetic substrates has been described.
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The Electrophoretic α;1-Globulin Pattern of Serum in α;1-Antitrypsin Deficiency

TL;DR: In this paper, the Electrophoretic α, 1-Globulin Pattern of Serum in α; 1-Antitrypsin Deficiency; and 1-Girdhar et al.
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The synthesis and analytical use of a highly sensitive and convenient substrate of elastase.

TL;DR: The synthesis and analytical use of succinyl-( l -alanine) 3 - p -nitroanilide, a new elastase substrate that is virtually not attacked by trypsin or chymotrypsin and does not undergo appreciable spontaneous hydrolysis is described.
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High recovery of tryptophan from acid hydrolysates of proteins

TL;DR: Moderate concentrations of thioglycolic acid largely prevented the destruction of tryptophan during acid hydrolysis of proteins.
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Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site.

TL;DR: Two tetrapeptide 4-nitroanilide substrates related to the reactive site of the plasma (~1’ protease inhibitor) were studied and indicate that oxidation of the PI Met of YePI is capable to destroying its reactivity toward most serine proteases.
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