Search PubMed⌕ Search

Biomedical subjects

P Mandel

Publications and source records attributed to P Mandel.

At least 361 records · Page 20Linked to original sources
PubMed1978

Superoxide dismutase activity in nerve cell culture.

Superoxide dismutase (EC 1.15.1.1) activity was assayed in preparations obtained from several clonal lines of nerve cell culture, by enzymatic and nonenzymatic assays. The enzyme was found in dialyzed homogenates of washed cells and in partially purified fractions. The enzyme was also found in cells which had been grown in media containing 5-bromodeoxyuridine, where cell differentiation was observed.

Astrocytoma↗
PubMed1978

Comparative study of miscellaneous properties of cysteine sulfinate transaminase and glutamate oxaloacetate transaminase in chick retina homogenate.

The activity, properties, and developmental pattern of cysteine sulfinate transaminase (CSA-T) were studied in chick retina and compared with the activity, properties, and developmental pattern of glutamate oxaloacetate transaminase (GOT). Their optimum pH is identical whereas the effect of pyridoxal phosphate seems to be different. Developmental patterns are also different. The Km and Vm of CSA-T and GOT were determined in chick retina homogenate. These results suggest that two different enzymes are responsible for the transamination of cysteine sulfinate (CSA) and aspartate.

Aging↗
PubMed1978

Ultrastructural localization study of two Wolfgram proteins in rat brain tissue.

The ultrastructural immunohistochemical localization of Wolfgram proteins W1 and W2 is described in young rat brain tissue. The labelling by the antiserum to W1 is restricted to oligodendroglial cells and myelin sheaths. The plasma membrane of the cells as well as the polysomes are positively stained whereas the mitochondria and the nuclei are always free of labelling. Glial cell processes with definite organelles, which are involved in the myelination of neighbouring axons, are also positive to the antiserum. In the myelin sheaths, the positive staining occurs predominantly at the dense period line of the innermost and outermost lamellae. The present results add further evidence for a specific local synthesis of these Wolfgram proteins in oligodendroglial cells during myelination.

Animals↗
PubMed1978

[Extraction and purification of tissue phosphopeptides].

We describe a method of extraction and partial purification of phosphopeptides isolated from pig brain or from the electrical organ of Torpedo marmorata. The extraction of the phosphopeptides was achieved by alcoholic 0,04 N potassium hydroxyde solution or by 10(-1) M KCL containing 10(-3) M EDTA and 10(-4) M DTT. After having tried various fractionation methods like ion exchange chromatography or gel filtration we chose chromatography on DEAE Sephadex followed by purification of the isolated fractions by Sephadex G 25 filtration. The most important phosphate fractions (one was purified to about 90 per cent) were characterized by the determination of the N/P ratio which was different from one phosphopeptide to another. The amino acid composition showed a high glycin, serine and "acid" amino acid content. The presence of phosphoserine was shown by electrophoresis and chromatography of a partial hydrolysate of in vivo 32P labelled phosphopeptides isolated from rat liver. The polyanionic structure of these phosphopeptides allow them to act as real ion exchangers which might be involved during active transport mechanisms in cellular membranes.

Amino Acids↗
PubMed1978

[Fatty acid distribution of the normal sciatic nerve lipids in the rat].

We isolated and purified the main lipids of the rat sciatic nerve. After methanolysis, fatty acids were isolated and purified by thin layer chromatography, and studied by gas chromatography. C 16 and C 18 fatty acids are the most abundant. Among the long-chain fatty acids, arachidonic acid (20:4) is present in some lipids; highly desaturated fatty acids in C 22 and C 24 are also present. In general, the fatty acids are highly saturated; cholesterol esters and ethanolamine phosphoglyceride fatty acids are highly unsaturated.

Animals↗
PubMed1978

Properties of partially purified bovine brain dopamine beta-hydroxylase.

Dopamine beta-hydroxylase has been partially purified from bovine brain. A 140-fold purification factor was achieved using solubilization with Triton X-100, ammonium sulphate fractionation between 20-50 per cent saturation, affinity chromatography on concanavalin A-Sepharose 4 B and then filtration through Sephadex G200. The specific activity at the end was 51 nmoles/h/mg protein. The majority of endogenous inhibitors were lost. Immunological studies, kinetic studies, studies on the interaction with lectins and the effect of carboxylic acids on enzyme activity were carried out. Our data are in favour of the close similarity between the bovine brain and adrenal enzymes. No major differences could be found, at least with the characterization experiments using in the present study.

Adrenal Glands↗
PubMed1978

RNA metabolism in M1 adrenergic neuroblastoma cells.

RNA metabolism of M1 adrenergic neuroblastoma cells was investigated in logarithmic proliferating, stationary and differentiated states. [3h] uridine labelling experiments showed that in the stationary phase (10 days of culture) the cells incorporated less radioactive precursors into RNA than in the logarithmic phase (3 days of culture). Cells differentiated by bromodeoxyuridine treatment were compared with proliferating cells. At short labelling time, the BrdU-treated cells incorporated more [3H] uridine in RNA than the controls. But when morphological differentiation became irreversible, the treated cells incorporated less [3H] uridine into RNA. Our results show that morphological differentiation by BrdU-treatment of neuroblastoma M1 cells is not accompanied by striking changes in RNA metabolism.

Adenosine↗
PubMed1978

Studies of soluble rat liver mitochondrial acid ATPases. II. Structural and immunological properties of ATPase 1.

We described previously the existence of a soluble ATPase activity in rat liver mitochondria [1]. The purification and catalytic properties have been described [2]. In a continuation of these experiments, we have studied the immunologic and structural properties of one molecular form of this enzyme : ATPase I. We have prepared the antiserum anti-ATPase I and demonstrated the purity of our enzyme preparation by immunodiffusion and immunoelectrophoresis. An immunohistochemical method also confirmed the localization of ATPase I in the soluble fraction of mitochondria. The molecular weight of ATPase I was measured by G 100 Sephadex gel filtration and was found to be 18,400; electrophoresis on polyacrylamide gels gave a value of 18,600. The pHi of ATPase I was found to be 7,2. Amino acid analysis showed high amounts of aspartic acid, glutamic acid, serine and glycine. The molecular weight calculated from the total amino acid residues was found to be 17,000. Alanine is the NH2 terminal amino acid. The peptide maps obtained after degrading ATPase I with cyanogen bromide or trypsin are in accordance with the methionine, lysine and arginine residues we found in the ATPase I molecule. ATPase I does not appear to be a glycoprotein.

Adenosine Triphosphatases↗
PubMed1978

Purification and some properties of L-glutamate decarboxylase from human brain.

Glutamate decarboxylase (EC 4.1.1.15) from human brain has been purified 8000-fold with respect to the initial homogenate. The molecular weight of the native enzyme was found to be 140000 by electrophoresis on a polyacrylamide gradient gel slab. The presence of a single protein band (Mr 67000) on sodium dodecylsulphate/polyacrylamide gel and the existence of only one N-terminal amino acid suggest that the enzyme consists of two similar if not identical polypeptide chains. The Km of the enzyme at the optimum pH of 6.8 is about 1.3 x 10(-3) M for glutamate and 0.13 x 10(-6) M for pyridoxal phosphate. The analysis of the effects of various inhibitors of mouse brain glutamate decarboxylase on the human enzyme confirms the strong competitive inhibition caused by 3-mercaptopropionic acid (Ki = 2.7 x 10(-6) M) while the Ki values for allylglycine and chloride ion are 1.8 x 10(-2) M and 2.2 x 10(-2) M, respectively.

Amino Acids↗