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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
|
pubmed:dateCreated |
1993-3-17
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pubmed:abstractText |
We found a cysteine proteinase inhibitor in human hair shaft extract treated with 0.01 M Tris HCl buffer, pH 8.0. A yield of 0.2 mg of purified cysteine proteinase inhibitor was obtained from 86 g of hair shaft. The cysteine proteinase inhibitor had a molecular mass of 13 kDa as determined by high-performance liquid chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis. It was more stable to heat and pH than most proteins and had a pI of 4.7. Immunologically, its antigenicity was the same as that of cystatin A, but differed from that of cystatin B and C, and kininogen. The amino-acid sequence of the first 30 residues from the NH terminus of the inhibitor was identical to that of cystatin A from human epidermis. Hair shaft cysteine proteinase inhibitor is thus considered to be identical to epidermal cystatin A.
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pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0340-3696
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
284
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
380-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1992
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pubmed:articleTitle |
Purification and characterization of a cystatin-type cysteine proteinase inhibitor in the human hair shaft.
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pubmed:affiliation |
Department of Hygiene, Kawasaki Medical School, Kurashiki, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study
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