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Two rat homologues of human cystatin C
Author(s) -
Esnard Annick,
Esnard Frédéric,
Faucher Didier,
Gauthier Francis
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80080-2
Subject(s) - cystatin , isoelectric point , cystatin c , concanavalin a , chemistry , biochemistry , urine , isoelectric focusing , homology (biology) , microbiology and biotechnology , glycoprotein , amino acid , biology , enzyme , in vitro , renal function
Two immunochemically related forms of cystatin C‐like inhibitors which differ in their M r app and isoelectric point have been found both in urine and seminal vesicles of rats. Amino‐terminal sequences of these two cystatins are identical within the same fluid and exhibit a high degree of homology with that of human cystatin C. However, cystatins C purified from urine lack eight residues at their amino‐terminal end when compared to those of seminal vesicles. The occurrence of two cystatin C‐like components in rat fluids has been found to be due to the presence of a glycosylated form reported here as cystatin Cg which specifically binds concanavalin A and is susceptible to endo‐β‐ N ‐acetylglucosaminidase treatment.