Purification and properties of rat liver cysteine sulfinate decarboxylase

Lin, Yuchen; Demeio, R. H.; Metrione, Robert M.

doi:10.1016/0005-2744(71)90256-7

Cited by 20 publications

(3 citation statements)

References 13 publications

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“…No immunolabeling was visible on the brain homogenate. (Lin et al, 1971;Guion-Rain et al, 1975), according to their purification procedure. It must be noted, however, that we did not isolate pure CSD in its native form.…”

Section: -mentioning

confidence: 99%

Specific Antiserum and Monoclonal Antibodies Against the Taurine Biosynthesis Enzyme Cysteine Sulfinate Decarboxylase: Identity of Brain and Liver Enzyme

Remy

Henry

Tappaz

1990

Journal of Neurochemistry

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Cysteine sulfinate decarboxylase (CSD), the putative biosynthetic enzyme for taurine, was purified 1,800-fold with a 1% yield from rat liver, where it was found to be 20-fold enriched compared with brain. The final fraction was homogeneous, as ascertained through sodium dodecyl sulfate-polyacrylamide gel electrophoresis and reverse-phase HPLC. An antiserum was raised in the rabbit that (a) quantitatively immunoprecipitated CSD activity and (b) immunolabeled only one band (MW = 51,000) on an immunoblot from liver homogenate. Monoclonal antibodies were also raised that recognized the CSD protein and immunolabeled the same 51-kilodalton protein on an immunoblot from liver homogenate. In a brain extract, two CSD activities had been previously found and named CSDI and CSDII, according to their chromatographic elution patterns. We have compared the properties of CSDI from brain--the most likely enzyme involved in the biosynthesis of taurine in the brain, according to previous investigations-and CSD from liver: Both activities (a) were similarly eluted on ion-exchange and hydroxyapatite chromatographies, (b) showed the same elution pattern on gel filtration with an apparent native molecular weight of approximately 63,000, and (c) were immunoprecipitated in a strictly identical manner by the antiserum against liver CSD. Moreover, this antiserum as well as the monoclonal antibodies immunolabeled a single band (51 kilodaltons) on an immunoblot from brain CSD-enriched fraction or liver fraction. All these data show that CSDI from brain and liver CSD are the same monomeric enzyme. They also indicate that a specific antiserum against rat liver CSD has been raised that can be used for immunocytochemical visualization of CSD-containing cells in the brain.

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Section: -mentioning

confidence: 99%

Specific Antiserum and Monoclonal Antibodies Against the Taurine Biosynthesis Enzyme Cysteine Sulfinate Decarboxylase: Identity of Brain and Liver Enzyme

Remy

Henry

Tappaz

1990

Journal of Neurochemistry

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“…A number of reports lend support to the occurrence of a single enzyme operating the decarboxylation of XI and XII, although at different rates (19-21). Some disagreement, however, has appeared at this regard (22). To our knowledge the possibility that glutamate decarboxylase could operate also the decarboxylation of XI and XII has not been eliminated.…”

Section: Chmentioning

confidence: 95%

Ambiguities in the enzymology of sulfur-containing compounds

Cavallinì¹,

Federici²,

Duprè³

et al. 1980

Pure and Applied Chemistry

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-The specificiations of enzymes towards sulphur-containing aminoacids ind some of their degradation products and derivatives are discussed.In the course of this meeting we have occasionally met reactions involving a variety of sulfur-containing compounds carried out by systems or enzymes also used for different purposes. In this final lecture we should like to point out how this phenomenon is much more general than believed, thus indicating the occurrence of a real ambiguity in the enzymology of sulfur'.containing compounds. This fact came to the attention of one of us early in 1956, when cystamine (I) and lanthionamine (II) were assayed as substrates for diamine oxidase (1). It was known at that time that diamine oxidase was an enzyme of broad specificity, being able to use as substrates diamines having different carbon chain lengths and also diamines with one of the amino groups substituted with an imidazole or a guanido group (2). However it was not known whether a substantial change of the chemical composition would have impaired the enzymatic attack on the substrate. It was therefore a surprise to find an enzyme unable to recognize the substitution of a methylene carbon of the substrate with one or two atoms of sulfur. Diamine oxidase uses not only I and II as substrates but also lanthionamine sulfone, although at a lower rate than I and II (1). The interest of this finding was increased by the observation that the rate of the oxidation of I and II was in the range of that of the traditional substrates and that the oxidation was followed by the cleavage of the intermediate cystaldimine (IV) leading to the formation of compounds of biological interest like thiocysteamine (VI), hypotaurine (VII), thiotaurine (VIII) and taurine (IX) (3-7). It is evident that diamine oxidase uses as reacting points the nitrogen-containing groups while the composition of the carbon chain between them could be radically modified to the point of being partially substituted with sulfur atoms without impairing the enzymatic attack.Cysteinesulfinic acid (XI) and cyteic acid (XII) are also known to take profit from a number of enzymes used for other purposes. In this case the group producing the ambiguity is the sulfinic or the sulfonic group which simulate the carboxyl group of the carbon analogs glutamic and aspartic acids. XI and XII are able to substitute glutamic and aspartic acids in the common transaminase reactions (8-11).The possible occurrence of a specific transaminase for XI (12) is yet to be substantiated by the isolation of the pure enzyme. We had the opportunity to use XI as substrate for mitochondrial aspartate amino transferase purified up to homogeneity thus confirming that this enzyme actually transaminates XI irrespective of the possible occurrence of a specific enzyme Other sulfur containing substrates for this transaminase are: (XIII to XV), cysteine-S-sulfonate (13), alanine thiosulfonate (14), and serine-O-sulfate (15). It is remarkable that while the enzyme uses XV as substrate, it is inactive towards...

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“…In addition, the soluble enzyme apparently has a lower requirement for the pyridoxal 5' -phosphate coenzyme. The enzyme has been purified from rat liver and from horse kidney (93)(94)(95)(96)(97)(98). The present consensus is that the same enzyme catalyzes the decarboxylation of cysteinesulfinic acid and of cysteic acid.…”

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confidence: 97%

Vitamin B-6 and Sulfur Amino Acid Metabolism

Sturman

1981

Methods in Vitamin B-6 Nutrition

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Purification and properties of rat liver cysteine sulfinate decarboxylase

Cited by 20 publications

References 13 publications

Specific Antiserum and Monoclonal Antibodies Against the Taurine Biosynthesis Enzyme Cysteine Sulfinate Decarboxylase: Identity of Brain and Liver Enzyme

Specific Antiserum and Monoclonal Antibodies Against the Taurine Biosynthesis Enzyme Cysteine Sulfinate Decarboxylase: Identity of Brain and Liver Enzyme

Ambiguities in the enzymology of sulfur-containing compounds

Vitamin B-6 and Sulfur Amino Acid Metabolism

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