By Katarzyna M. Dziegielewska Ph.D., William M. Brown Ph.D. (auth.)
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112. Omori-Satoh T. Antihemorrhagic factor as a proteinase inhibitor isolated from the serum of Trimeresurus flavouiridis. Biochem Biophys Acta 1977; 495:93-98. 113. Yamakawa Y, Omori-Satoh T. An improved method for purifying antihemorrhagic factor in the serum of Habu snake ( Trimeresurus jlavoviridis). J Biochem 1991; 110:767-769. 114. Campbell A, Wicha MS, Long M. Extracellular matrix promotes the growth and differentiation of murine hematopoietic cells in vitro. J Clin Invest 1985; 75:2085-2090.
39 Three sequences of the form gly-xaa-pro were noted. In addition, two potential sites for proline hydroxylation ala267-pro-gly and prozs6-pro-gly, in agreement with the consensus acceptor sequence of prolyl hydroxylases, 174 were described. A single site (prozs1-pro-gly) is also present in pig fetuin, 18·22 though not in sheep, bovine, rat or mouse fetuin (Fig. 1) raising doubts as to its significance. 175 It has also been reported that human cystatin C (also referred to as a-trace in older literature) is partially hydroxylated on pro3 (see ref.
PROTEOLYTIC SITES A proteolytic cleavage site was first identified in human fetuin by Lebreton et al; 28 the purified protein was described as being "fragile," readily breaking into three pieces of 30 kDa, 6 kDa and 4. 7 kDa. Structure of the Fetuins 27 From more recent analysis, 34 the trypsin-sensitive site has been assigned; it is a typical dibasic cleavage site (arg12s-lys) next to the D 1/D2 interdomain junction (see Figs. 4). We identifiied and characterized the corresponding cleavage site in bovine fetuin, 15 •16 and the same site is present in rat/ 1 sheep 18 and mouse fetuins 74•77 (see Fig.
