Bisalbuminemia associated with albumin dye binding defect

CLINICA CHIMICA ACTA

579

CGA 4850

Bisalbuminemia

associated

with

albumin

dye binding

defect

Risalbuminemia is the presence of two electrophoreticallg different albumins and has been demonstrated to be an inheritable trait in several family studiesI-*. One study has demonstrated a defect in thyroxine binding by the abnormal albumin. This anomaly may exist as being one of two types depending on the relative mobility of the abnormal albumin. Weir& has suggested that the symbol AFL be used in naming the albumin slower than normal, and Al RA to be used in naming the abnormal component if it is faster than normal. In the case described here the abnormal albumin is of the AlsL type. During the laboratory evaluation of a previously healthy, elderly male patient who was hospitalized because of a cerebrovascular accident, a bisalbumin of the slow variety was detected by cellulose acetate electrophoresis (Fig. I). It was noted that the albumin value as determined by electrophoresis did not correlate with that of the IIARA dye method?, However, further investigation revealed that the electrophoretic albumin value did agree with the value obtained from a bromcresol green methods. The difference between the two chemically determined values was in accord with the amount of bisalbumin present by electrophoresis (Table I). The Ouchterlony agar diffusion technique and immunoelectrophoresis using antihuman albumin goat serum identified the abnormal protein as albumin. Using antihuman polyvalent goat sera the immunoelectrophoretic pattern showed a similar double albumin band as was obtained using specific anti-albumin. Studies with human iulmunoglobulin anti-sera ruled out any possibility of paraproteinemia associated

Fig. I. ~lectrophoretic separation of patient’s serum (top) with a densitometric scram (below) is used as a reference.

tracing. Normal

C&z. Claim. Acta, 36 (1972)

j79-580

BRIEF

580 TABLE

NOTES

I

TOTALSERUM

ALBUMIN

ASDETERMINED

Method of determination

Albumin

(g/loo

Electrophoresis HABA dye B.C.G. dye

3.1 (AlN 2.1

=

BYDIFFERENTMETHODS ml)

1.9, AW

=

1.2)

3.3

with

this albumin variant. The bisalbumin persisted in multiple samples obtained over a month’s period, and did not disappear upon storage.9 Heat inactivation of the serum at 56” for 30 min failed to alter the electrophoretic pattern. Family members were not available for testing. The studies suggest that the albumin binding sites for HABA dye and B.C.G. are not identical. These possibilities are under current investigation. Department Milwaukee Milwaukee,

of Pathology, County General Hospital, Wise. 53226 (U.S.A.)

T. A. RI. J. &I.

HOSTY CAPUTO

HOLLENBECK

A. KASAMAKI, T. BEN-P• RAT, AND A. S. KAPLAN, Nature, 217 (1968) 759. M. EARLE, P. HUTT, K. SCHMID AND D. GATLIN, J. Clin. Invest., 3X (1959) 1412. E. J. SARCIONE AND C. W. AUNGST,B~OO~, 20(1962) 156. K. J. WEIME, Clin. Chim. Acta, 5 (1960) 443. E. J. SARCIOKE AND C. W. AUNGST, Clin. Chim. Acta, 7 (1962) 297. R. J. WEIME AND H. PETERS, Protides of theBiologicalFluids, Proceedings of the 9th Colloquium, Bruges, 1961, Elsevier, Amsterdam 1962, p. 221. 7 Technicos autoanalyzer method N-15c, Technicon Instruments Corp., Terrytown, N.Y. 10015. 8 B.T. DOUMAS,~. A.WATSON AND H.G.BIGGs,CZ~. Chim. Acta, 31 (1971) 87. 9 T. ARENDS, M. L. GALLANGO, M. LAYRISSE, J. WILBERT APED H. D. HEINES, Blood, 33 (1969)

I 2 3 4 5 6

114.

Received Gin.

October

Chim. Acta,

I, 1971

36 (1972) 579-580

ERRATUM

In the 1972 January

issue, page 275, correct in the titel EDNA to EDTA.