Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver
Biochemical and Biophysical Research CommunicationsPublished 1 September 1985
Anka Ritonja, Werner Machleidt, A. John Barrett
Citations105
SJR quartileQ2
SJR score0.75
SNIP0.56
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TL;DR
The complete amino acid sequence of the cysteine proteinase inhibitor cystatin B (formerly named CPI-B) from human liver was determined by automated solid-phase Edman degradation of a large cyanogen bromide fragment and peptides generated by enzymatic cleavage.
Abstract
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 (Mr = 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 beta from rat liver, but contains only a single cysteine. Human cystatin B is able to form a dimer stabilized by noncovalent forces.
Keywords
Agricultural and Biological SciencesBiochemistry, Genetics and Molecular Biology
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