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Biomedical subjects

B Straus

Publications and source records attributed to B Straus.

At least 19 recordsLinked to original sources
PubMed1992

Arginase, a new marker of mammary carcinoma.

Activities of arginase, alanine aminotransferase, aspartate aminotransferase and alkaline phosphatase were determined in sera obtained in a group of healthy women, women with verified carcinoma of the breast, benign mastopathy, a group of patients with carcinoma of various organs and a group of patients with acute viral hepatitis. Preoperative values of serum arginase activity in patients with breast carcinoma were up to 4-fold those found in healthy women. Sensitivity of the test was 86%. After the surgery, the activity decreased abruptly during the first week and normalised within 15-30 days. In benign diseases of the breast, the activity of arginase was normal. Serum arginase activity is raised in both benign and malignant liver diseases, however, the quotients alanine aminotransferase/arginase, aspartate aminotransferase/arginase and alkaline phosphatase/arginase differ significantly. Thus, use of alanine aminotransferase/arginase quotient implies a high degree of confidence in differentiating between increased arginase activity in mammary carcinoma (alanine aminotransferase/arginase = 0.572 +/- 0.278) and high arginase activity in hepatitis (alanine aminotransferase/arginase = 12.226 +/- 1.822).

Adult↗
PubMed1990

Multiple forms of gamma-glutamyltransferase and lipoproteins.

The gamma-glutamyltransferase isoenzyme patterns originating from human serum and homogenates of liver, kidney, pancreas and intestine in the presence and in absence of isolated lipoproteins has been studied. On the basis of these results one can conclude that the distribution of a variety of gamma-glutamyltransferase activities obtained by the electrophoresis of blood serum is not a consequence of an existence of a large number of true isoenzymes, but of increased concentrations of lipoproteins which bind to the enzyme thus causing the appearance of gamma-glutamyltransferase in the region of the appropriate lipoproteins.

Humans↗
PubMed1989

A simple and fast method for iron determination with ferrozine after proteolytic disruption of iron-transfer in complex.

A direct method for iron determination with ferrozine in blood serum is described. Iron is liberated and proteins degraded by pepsin in hydrochloric acid medium. At appropriate pH the iron-ferrozine complex forms and stabilizes in five minutes. Accuracy of the method is 99.3-101.4%, precision within run and day to day 0.73 and 1.1% respectively, and linearity till 72 mumol/L iron.

Adult↗
PubMed1989

Changes of activities of some transferases, alkaline phosphatase and cholinesterase in the blood of women using oral contraceptives and in vitro influence of these agents on tissular enzyme levels in rat liver.

Aspartate aminotransferase, alanine aminotransferase, gamma-glutamyltransferase, and alkaline phosphatase activities in the blood serum of women taking the oral contraceptive preparation Microgynon through extended periods were raised; the activity of cholinesterase was simultaneously reduced. In rats liver homogenates ethynylestradiol, one of the active components of Microgynon, acted as an inducer of gamma-glutamyltransferase and alkaline phosphatase while leaving aspartate aminotransferase and alanine aminotransferase unaffected, but reduced the level of cholinesterase. Norgestrel, the other active component of the preparation, suppressed the biosynthesis of gamma-glutamyltransferase and alkaline phosphatase while leaving aspartate aminotransferase, alanine aminotransferase and cholinesterase levels unaffected. A mixture of ethynylestradiol plus norgestrel in the mass proportion occurring in Microgynon produced the same effects upon gamma-glutamyltransferase and alkaline phosphatase as ethynylestradiol alone. Estradiol, the parent hormone of ethynylestradiol, lacked the inducing capability of the latter while ethynylpropargyl chloride induced gamma-glutamyltransferase and alkaline phosphatase so it was concluded the inducing effect of ethynylestradiol must be ascribed to the ethynyl radical. Progesterone, the parent of norgestrel, shared the latter's suppressive activity for gamma-glutamyltransferase and alkaline phosphatase biosynthesis, and behaved like its derivative towards the other enzymes.

Adult↗
PubMed1981

Effect of sodium tetrathionate on the activities of some enzymes in kidney and urine.

The activities of lactate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase, beta-galactosidase, N-acetyl-beta-D-glucosaminidase, leucine aminopeptidase, gamma-glutamyltransferase and alkaline phosphatase in renal tissue and urine of rats treated with sodium tetrathionate were determined. A decrease of enzyme activities in renal tissue and an increase in urine were observed. The largest decrease in the glutamate dehydrogenase of renal tissue amounted to 0.7 times the control value, and was correlated with an appropriate increase in the urine. Increases in urinary enzyme activity were especially marked for beta-galactosidase and N-acetyl-beta-D-glucosaminidase (3 and 6 times the control values, respectively). The increase in enzyme activities was not accompanied by a corresponding change in the urinary protein. Characterization of urinary lactate dehydrogenase and N-acetyl-beta-D-glucosaminidase isoenzymes also indicates the renal origin of these enzymes. The abnormally high enzyme activities of the urine correlated with the nature and degree of renal damage shown by electron microscopy.

Acetylglucosaminidase↗
PubMed1976

Separation of arginase isoenzymes from human tissues by agar gel electrophoresis.

Arginase (EC 3.5.3.1) from human liver. kidney, mammary gland, and erythrocytes, was separated by agar-gel electrophoresis using barbital buffer pH 8.6. Three isoenzymes were separated. Two of these, A2 and A3, occur in liver and erythrocytes. The same two isoenzymes were found in the kidney, but in reversed proportions. In addition to the A3 isoenzyme, the mammary gland contains a fast anodically moving A1 isoenzyme. The three isoenzymes differ in their degree of sensitivity to ornithine.

Arginase↗
PubMed1975

T rosettes in alcoholic cirrhosis of the liver.

Thirty patients with alcoholic cirrhosis of the liver were studied for in vivo and in vitro correlates of cellular immunity. Seventy-seven percent failed to be sensitized to dinitrochlorobenzene, indicating impairment of the in vivo cellular immune response. A significant decrease in the number of T-rosette-forming cells was observed in this group of patients (.01 smaller than P smaller than .025). This finding suggests that the active T-rosette test is a valuable tool in detecting partial alterations in cell-mediated immunity in alcoholic cirrhosis of the liver. Our results also suggest that rosette formation is a more sensitive indicator of cell-mediated immunity than phytohemagglutinin-stimulated blastogenesis in patients with alcoholic cirrhosis of the liver.

Alcoholism↗