Stability of alpha 1-microglobulin, beta 2-microglobulin and retinol binding protein in urine.
The stability of alpha 1-microglobulin (alpha 1M), beta 2-microglobulin (beta 2M) and retinol binding protein (RBP) in urine was determined in 135 random samples from children with renal disease, febrile illness, malignancy, and from controls. Immediately after voiding, samples were divided into two portions, one of which was alkalinized. After identical transit times and laboratory handling the pH and concentrations of the individual proteins in each pair were measured. beta 2M was unstable in urine of pH less than 7 and grossly so below pH 6. In some instances beta 2M was low or undetectable even in the alkalinized samples when alpha 1M and RBP levels were raised, suggesting that degradation of beta 2M may have occurred prior to voiding. Concentrations of alpha 1M and RBP were significantly lower in the non-alkalinized fractions at pH less than 7, although to lesser degree than for beta 2M. Contrary to previous reports, we conclude that the stability of all 3 proteins is affected by urinary pH and recommend that this be measured and alkalinisation performed at the time of voiding.
Donaldson
M D
MD
Royal Hospital for Sick Children, Bristol, UK.
Chambers
R E
RE
Woolridge
M W
MW
Whicher
J T
JT
D000510:Alpha-Globulins / Q000652:urine*; D002648:Child; D006801:Humans; D006863:Hydrogen-Ion Concentration; D012177:Retinol-Binding Proteins / Q000652:urine*; D001613:beta 2-Microglobulin / Q000652:urine*
D000510:Alpha-Globulins; D012177:Retinol-Binding Proteins; C016001:alpha-1-microglobulin; D001613:beta 2-Microglobulin