Non-enzymatic glycation of human albumin does not alter its palmitate binding.

The study described here makes use of a new technique to assess the level of non-enzymatic glycosylation (glycation) by purified radioactively labelled glucose. Glycation up to 3 molglc/mol protein of human serum albumin, in contrast to previous reports, did not affect the binding of up to 2 mol palmitate, which was reached at a ratio of 7.5 palmitate/HSA. The uptake of palmitate from albumin by either erythrocytes or HL-60 cells also was not influenced by glycation of 3 mol glucose/mol protein. The distribution of palmitate into neutral lipids, phospholipids, or the palmitate designated for oxidation was likewise not influenced. This suggests that levels of albumin glycation likely to be encountered in the blood of diabetic subjects (up to 1 molglc/mol HSA) do not affect fatty acid utilization.