Retinol binding protein prepared from human urine was fractionated by chromatofocusing into four isoforms: two retinol-containing (holo-) and two retinol-free (apo-) species. The pl values of the isoforms ascertained by isoelectrofocusing with an immobiline pH gradient were: holo(I) 4.79-4.77; apo(II) 4.61-4.56; holo(III) 4.63 and apo(IV) 4.46-4.41. In vitro aging experiments with apo(II) under conditions favoring deamidation (37 degrees C, pH 7-10, 3-28 days) resulted in formation of the more acidic apo(IV)-isoform. The aging rate was consistent with pH increase. It appears that the urinary RBP mixture is composed of two apo-holo pairs: a native form with genuine protein structure and an acidic form generated upon aging.
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