Purification and characterization of a cystatin-type cysteine proteinase inhibitor in the human hair shaft.
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.
Tsushima
H
H
Department of Hygiene, Kawasaki Medical School, Kurashiki, Japan.
Ueki
A
A
Mine
H
H
Nakajima
N
N
Sumi
H
H
Hopsu-Havu
V K
VK
D015891:Cystatins / Q000032:analysis* / Q000302:isolation & purification*; D004817:Epidermis / Q000737:chemistry*; D006197:Hair / Q000737:chemistry*; D006801:Humans
D015891:Cystatins