| pubmed-article:311784 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:311784 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:311784 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:311784 | lifeskim:mentions | umls-concept:C0030306 | lld:lifeskim |
| pubmed-article:311784 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:311784 | lifeskim:mentions | umls-concept:C1418544 | lld:lifeskim |
| pubmed-article:311784 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:311784 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:311784 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:311784 | pubmed:dateCreated | 1979-6-29 | lld:pubmed |
| pubmed-article:311784 | pubmed:abstractText | The interaction of the human plasma protein, alpha-1-antitrypsin, with porcine pancreatic elastase was studied by isolating and characterizing their reaction products. Native alpha-1-antitrypsin has a mass ratio (Mr) of 54,000, an amino-terminal glx, and a carboxy-terminal lys residue. The elastase used has an Mr of 26,400 and an amino-terminal val residue. When the two proteins are combined at inhibitor excess, two major products result. One of the products is a complex of the enzyme and inhibitor with amino-terminal ser and val residues, which indicates that a peptide has been removed from the amino-terminal end of the inhibitor. The second product is a modified form of alpha-1-antitrypsin with an Mr of 51,300, an aminoterminal glx residue and a carboxy-terminal thr-leu dipeptide. It has no inhibitory activity against elastase. The components of the isolated complex can be split at high pH in the presence of diisopropyl fluorophosphate, which results in a catalytically inactive enzyme with the same Mr and amino-terminal residue as the native enzyme, and a large fragment of alpha-1-antitrypsin (alpha-1-antitrypsin(*)). This fragment has an Mr of 50,100, an amino-terminal ser residue and a carboxy-terminal thr-leu dipeptide. Based on these data, the following hypothesis is proposed. Elastase can attack alpha-1-antitrypsin at either of two major sites. If it attacks first at the carboxy side of the thr-leu dipeptide, located in the carboxy-terminal portion of the inhibitor, the alpha-1-antitrypsin is cleaved into two fragments with loss of inhibitory activity and absence of complex formation. If, however, the elastase first attacks an x-ser bond near the amino-terminal end of the inhibitor, the elastase then reacts with alpha-1-antitrypsin at the same leu moiety to form a stable complex with complete inhibition of the enzyme. | lld:pubmed |
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| pubmed-article:311784 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:311784 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:311784 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:311784 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:311784 | pubmed:issn | 0021-9738 | lld:pubmed |
| pubmed-article:311784 | pubmed:author | pubmed-author:CohenA BAB | lld:pubmed |
| pubmed-article:311784 | pubmed:author | pubmed-author:JamesH LHL | lld:pubmed |
| pubmed-article:311784 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:311784 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:311784 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:311784 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:311784 | pubmed:pagination | 1344-53 | lld:pubmed |
| pubmed-article:311784 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:311784 | pubmed:meshHeading | pubmed-meshheading:311784-a... | lld:pubmed |
| pubmed-article:311784 | pubmed:year | 1978 | lld:pubmed |
| pubmed-article:311784 | pubmed:articleTitle | Mechanism of inhibition of porcine elastase by human alpha-1-antitrypsin. | lld:pubmed |
| pubmed-article:311784 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:311784 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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