A Proteoglycan Related to the Urinary Trypsin Inhibitor (UTI) Links the two Heavy Chains of Inter-α-Trypsin Inhibitor
- 1 January 1989
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 370 (1) , 329-336
- https://doi.org/10.1515/bchm3.1989.370.1.329
Abstract
CDNA studies have suggested that inter-.alpha.-trypsin inhibitor (ITI) is a complex of several different peptide chains; the sequence of the inhibitory part of ITI is in excellent agreement with that of the urinary trypsin inhibitor (UTI). The present report demonstrates that a compound immunologically related to UTI is released by digestion with porcine pancreatic elastase or human leucocyte elastase. Since UTI has been shown to be a proteoglycan, ITI has been treated by chondroitinase. In these conditions, ITI is dissociated and gives rise to two heavy chains (78 and 85 kDa) and one light chain (26 kDa) immunologically related to UTI and which PAGE moves close to UTIc (produced by chondroitinase treatment of URI) we suggest that ITI is non-covalent complex comprising two heavy chains and one light chain immunologically related to UTI and which is also a proteoglycan.This publication has 4 references indexed in Scilit:
- Plasma proteins immunologically related to inter-α-trypsin inhibitorBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- The Effect of the Glycosaminoglycan Chain Removal on some Properties of the Human Urinary Trypsin InhibitorBiological Chemistry Hoppe-Seyler, 1987
- cDNA Cloning of Human Inter-α-Trypsin Inhibitor Discloses Three Different ProteinsBiological Chemistry Hoppe-Seyler, 1987
- In vivo metabolism of inter-α-trypsin inhibitor and its proteinase complexes: Evidence for proteinase transfer to α2-macroglobulin and α1-proteinase inhibitorArchives of Biochemistry and Biophysics, 1986