✦ LIBER ✦

Association of microcystin-LR and its biotransformation product with a hepatic-cytosolic protein

✍ Scribed by Robinson, Nancy A. ;Matson, Charles F. ;Pace, Judith G.

Publisher: John Wiley and Sons
Year: 1991
Tongue: English
Weight: 967 KB
Volume: 6
Category: Article
ISSN: 0887-2082
DOI: 10.1002/jbt.2570060303

No coin nor oath required. For personal study only.

✦ Synopsis

Microcystin-LR (MCYST-LR), a cyclic peptide hepatotoxin, associates with high-molecularweight, liver cytosolic components. Repetitive cycles of heat denaturation and pronase digestion released 80 ? 6% of the bound radiolabel from these components, parent toxin (22% ), and two biotransformation products, with high-performance liquid chromatography (HPLC) retention times of 6.7 (52%) and 5.6 (13%) min. Both parent and the biotransformed (6.7 min) toxin appeared to be covalently bound to a monomeric protein of molecular weight 40,000 (protein plus radiolabeled toxin). Binding and biotransformation reactions were time-and temperature-dependent and did not require endogenous molecules <6,000 daltons. The binding appeared to be saturable with a maximum of 20 pmol MCYST-LR bound per mg protein.

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