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J P Bali

Publications and source records attributed to J P Bali.

8 recordsLinked to original sources
PubMed1978

[Radiocompetitive assay of sulfamido-3-chloro-4-benzoic acid with carbonic anhydrase as binding reagent (author's transl)].

The control of patients treated by diuretic sulfonamides can be carried out by a radiocompetitive assay using their binding properties to carbonic anhydrase (CA). In this paper we have studied the assay of sulfamido-3-chloro-4-benzoic acid (SD3) using dialysis equilibrium as separation procedure. With (CA) 2 X 10(-6) M and 14C-SD3 0.5 X 10(-6) M (specific activity: 2 muCi/mg), can be detected 0.5 X 10(-6) M of (SD3) in the assay medium. 6.5 mg protein present in serum lower the assay sensitivity twenty times, owing to an elevated value of the affinity constant, Ka, of albumin-(SD3) complex (10(3) mol-1). On the other hand, the molecules with sulfamidobenzoic group cannot be differentiated in this procedure.

Binding Sites↗
PubMed1977

[On GLC of bile acids in serum and bile (author's transl)].

Some modifications to previous methods are reported in this paper to make this chromatographic assay more specific and more specific and more convenient in practice. 1. Bile acids were deconjugated via an enzymatic route with choloylglycine hydrolase (EC 3.5.1.24). 2. By acetylation of methyl derivatives, chromatography on alumina which led to a loss of lithocholic acid, can be supressed. Moreover, the compounds obtained are thermically more stable than those obtained by trifluoroacetylation. 3. The use of nor-cholic acid as internal standard led to a better quantitation of bile acids than others because its relative retention time is located between cholic and chenodesoxycholic acid. 4. Because of the hight sensitivity of this method, the assay of duodenal samples can be made with minimal volumes (0.1 ml) allowing a direct extraction by organic solvents.

Amidohydrolases↗
PubMed1976

Presence of blood group H antigen on a carcinoembryonic antigen, and its enzymatic modification into blood group A and B specificities.

A carcinoembryonic antigen (CEA-M) was purified from a hepatic metastasis obtained from a blood group O patient with cancer of the rectum. Using 125I-labeled carcinoembryonic antigen (CEA) and blood group antisera, H specificity has been found on the CEA-M. As the addition of anti-H to anti-CEA does not modify the extent of binding of labeled CEA-M to its antibodies (86%), the H and CEA determinants are carried by the same molecule. The affinity chromatography of CEA-M on an immunosorbent "anti-H-Sepharose" demonstrated that a proportion of CEA-M molecules might bear both H and CEA antigenic determinants. In addition, glycosyltransferases were used to modify the blood group H specificity into blood group A or B specificities.

ABO Blood-Group System↗
PubMed1975

[Presence of the H blood group antigen on a carcinoembryonic antigen (CEA). Enzymatic transformation of H to A and B specificities].

The carcinoembryonic antigen (CEA-M) was purified from a hepatic metastasis obtained from a blood group O patient with a cancer of the rectum. Using 125I-labelled-CEA and blood group antisera, H specificity was found on the CEA-M; the addition of anti-H to anti-CEA does not modify the binding of labelled-CEA-M to its antibodies (86%), this result leads us to conclude that H and CEA determinants are carried by the same molecule. However the low percentage of binding (30% with 1/10 anti-H) suggests that only a few CEA-M molecules do carry the H antigenic determinant. Finally, glycosyltransferases were used to modify the H specificity into blood group A and B specificities.

ABO Blood-Group System↗