Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver

The complete amino acid sequence of the cysteine proteinase inhibitor cystatin B (formerly named CPI-B) from human liver was determined. The 98-residue sequence (M r = 11,175) was obtained by automated solid-phase Edman degradation of a large cyanogen bromide fragment and peptides generated by enzym...

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Veröffentlicht in:Biochemical and biophysical research communications 1985-09, Vol.131 (3), p.1187-1192
Hauptverfasser: Ritonja, Anka, Machleidt, Werner, Barrett, Alan J.
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Sprache:eng
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Zusammenfassung:The complete amino acid sequence of the cysteine proteinase inhibitor cystatin B (formerly named CPI-B) from human liver was determined. The 98-residue sequence (M r = 11,175) was obtained by automated solid-phase Edman degradation of a large cyanogen bromide fragment and peptides generated by enzymatic cleavage. The protein starts with a blocked Met-Met sequence which is presumably N-acetylated. The sequence shows that human cystatin B is a member of the family of intracellular cystatins; it is 79% identical with cystatin β from rat liver, but contains only a single cysteine. Human cystatin B is able to form a dimer stabilized by noncovalent forces.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(85)90216-5