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Title: Human tissue factor contains thioester-linked palmitate and stearate on the cytoplasmic half-cystine

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00412a004· OSTI ID:6904801

The state of the five half-cystine residues in human tissue factor (TF) has been characterized. The results indicate that the four half-cystines in the extracellular domain of TF form two disulfide bonds and the half-cystine in the cytoplasmic region is acylated by plamitic acid and stearic acid. The extracellular disulfide cross-links, Cys/sup 49/-Cys/sup 57/ and Cys/sup 186/-Cys/sup 209/, were deduced from the analysis of tryptic peptides. Acylation of the cytoplasmic half-cystine was demonstrated by purifying and characterizing fibroblast TF from cells labeled with (/sup 3/H)palmitic acid. Radiolabeled fibroblast TF was observed by autoradiography following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The tritiated material covalently bound to the protein was identified as (/sup 3/H)palmitate and (/sup 3/H)stearate by reverse-phase high-pressure liquid chromatography. Deacylation of TF with hydroxylamine resulted in the spontaneous generation of disulfide-linked TF dimers. This result suggests that the disulfide-linked TF dimer, a minor component of most TF preparations, and the recently described heterodimeric form of TF are artifacts produced by deacylation of Cys/sup 245/ and subsequent interchain disulfide bond formation.

Research Organization:
Mt. Sinai School of Medicine of the City Univ. of New York, NY (USA)
OSTI ID:
6904801
Journal Information:
Biochemistry; (United States), Vol. 27:12
Country of Publication:
United States
Language:
English