Sandbox Reserved 596: Difference between revisions
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'''PZ''' | '''PZ''' | ||
[[Image: | [[Image:Figure 1.JPG]] | ||
Bovine PZ was first identified by Prowse and Esnouf in 1977 and human PZ, consisting of 360 amino acid residues and having a molecular weight of 62kDa, was first isolated and studied by Broze Jr. and Miletich in 1984. The gene coding for human PZ, PROZ, was found in 1998 on chromosome 13 at location 13q34 and is composed of a 389 bp promoter and nine exons (one being an alternative exon). [1,4] PZ is a single-chain glycoprotein with a 13 γ-carboxyglutamic (residues 7, 8, 11, 15, 17, 20, 21, 26, 27, 30, 33, 35 and 40) acid residues (Gla) N-terminal domain (residues 1-46), two epithelial growth factor (EGF)-like domains (EGF1 residues 47-830, EGF2 residues 85-126), and a C-terminal serine protease (SP)- like domain (residues 135-360) (Figure 1). | Bovine PZ was first identified by Prowse and Esnouf in 1977 and human PZ, consisting of 360 amino acid residues and having a molecular weight of 62kDa, was first isolated and studied by Broze Jr. and Miletich in 1984. The gene coding for human PZ, PROZ, was found in 1998 on chromosome 13 at location 13q34 and is composed of a 389 bp promoter and nine exons (one being an alternative exon). [1,4] PZ is a single-chain glycoprotein with a 13 γ-carboxyglutamic (residues 7, 8, 11, 15, 17, 20, 21, 26, 27, 30, 33, 35 and 40) acid residues (Gla) N-terminal domain (residues 1-46), two epithelial growth factor (EGF)-like domains (EGF1 residues 47-830, EGF2 residues 85-126), and a C-terminal serine protease (SP)- like domain (residues 135-360) (Figure 1). | ||
