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B Straus

Publications and source records attributed to B Straus.

9 recordsLinked to original sources

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

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

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

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