Purification and characterization of a cystatin-type cysteine proteinase inhibitor in the human hair shaft.
Arch Dermatol Res
; 284(7): 380-5, 1992.
Article
en En
| MEDLINE
| ID: mdl-1288417
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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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cistatinas
/
Epidermis
/
Cabello
Límite:
Humans
Idioma:
En
Revista:
Arch Dermatol Res
Año:
1992
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Alemania