Structural insights into human serum albumin‐mediated prostaglandin catalysis

• DOI: 10.1110/ps.28702
• Publication Date: 2002-07-26T23:59:58Z
• Authors: Jinsheng Yang; Charles E. Petersen; Chung‐Eun Ha; Nadhipuram V. Bha...
• Keywords: Human albumin; Serum Albumin

Abstract Previous studies have shown that many arachidonic acid metabolites bind to human serum albumin (HSA) and the metabolism of these molecules is altered as a result binding. The present study attempted gain insights into mechanisms by which prostaglandins bound subdomain 2A HSA are metabolized catalytic processes. breakdown prostaglandin 15‐keto‐PGE 2 15‐keto‐PGA 15‐keto‐PGB in presence wild‐type number mutants was examined using previously validated spectroscopic method monitors absorbance at 505 nm. species this were HSA, K195M, K199M, F211V, W214L, R218M, R218P, R218H, R222M, H242V, R257M, bovine albumin. HSA‐mediated catalysis indicated HSA‐bound results from an alkaline microenvironment binding site. Our show two specific processes modulated amino residues. Specifically, some residues modulate rate step 1, conversion , while other 2, . Some steps 1 2. In total, our support involvement certain basic catabolism data suggest may be more complex process than thought.