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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Ritonja A,Machleidt W,Barrett AJdoi
10.1016/0006-291x(85)90216-5subject
Has Abstractpub_date
1985-09-30 00:00:00pages
1187-92issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(85)90216-5journal_volume
131pub_type
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