William R. Bergren

An improved electrophoretic procedure for galactose-l-phosphate uridyl transferase: Demonstration of multiple activity bands with the duarte variant☆

Abstract An improved electrophoretic procedure for erythrocyte galactose-l-phosphate uridyl transferase is described. A three-banded pattern was found by this method for Duarte variant individuals in contrast to a single band for normal individuals. This electrophoretic procedure also provides a means of distinguishing the Duarte variant homozygotes from the heterozygotes.

GALACTOSE-1-PHOSPHATE URIDYLTRANSFERASE ASSAY BY USE OF RADIOACTIVE GALACTOSE-1-PHOSPHATE.

Abstract 1. 1. A procedure for assay of galactose-I-phosphate uridyltransferase employing [I-14C]galactose-I-phosphate has been described. 2. 2. The method is direct, convenient and reproducible. It is applicable to diagnosis of galactosemia and is useful in family studies. 3. 3. Downs syndrome patients were found to have galactose-I-phosphate uridyltransferase values higher than normal, but the results were not in accord with a hypothesis localizing the gene for the enzyme in chromosome 21.

Galactonic Acid in Galactosemia: Identification in the Urine

Galactose is converted to galactonic acid in vivo in man. Galactonate was isolated from the urine of galactosemia patients who had been given galactose orally. The identity of the galactonate was established by gas-liquid chromatography and by the preparation of derivatives.

Uridine diphosphate galactose 4-epimerase in human and other mammalian hemolysates

Abstract 1. 1. In contrast to the requirement for exogenous NAD+ in the assay of UDP-galactose 4-epimerase (UDPgalactose epimerase, EC 5.1.3.2), in hemolysates from adults, substantial epimerase activity can be demonstrated in hemolysates from newborn infants without addition of NAD+. It has been shown that erythrocytes of newborns are deficient in stromal NAD nucleosidase; and that a considerable portion of intracellular NAD+ remains in the hemolysate. In the preparation of hemolysates of adults, NAD+ of intracellular origin is destroyed by activity of stromal NAD nucleosidase. 2. 2. Upon starch gel electrophoresis, two distinctly separate activity bands were found for epimerase in hemolysates from newborn infants and one distinct band, of different mobility, for the enzyme in hemolysates of adults. In the presence of NAD+ in the gel, electrophoresis of hemolysates of adults resulted in the two-banded epimerase pattern found for newborns. It is presumed that an NAD+-dependent structural change in the enzyme is involved. 3. 3. Two-banded electrophoretic patterns for epimerase were found in hemolysates of a number of mammals other than man, each set having a different electrophoretic mobility from that of any other.

Fucosidosis: Clinical, Pathologic, and Biochemical Studies of Five Patients

Fucosidosis is an inherited metabolic disorder in which deficiency of a-1-fucosidase activity results in accumulation of fucosyl compounds in lysosomes (6, 7, 24). Clinical manifestations reported include progressive motor and mental deterioration, coarseness of facial features, cardiomegaly, hepatomegaly, skeletal abnormalities and short stature (1,5,6,8,13). Initially many of the patients exhibit hypotonia, but progressive spasticity develops with time.