Purification and identification of hog-kidney histaminase

Kapeller-Adler, Regine; MacFarlane, H.

doi:10.1016/0926-6569(63)90276-1

Cited by 45 publications

(9 citation statements)

References 42 publications

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“…Spectral properties of the enzyme. It has previously been shown (Eady & Large, 1968) that the substrate specificity and inhibitor pattern of the 766 1971 primary amine dehydrogenase of Pseudomonas AM1 are similar to those of the 'diamine oxidase' ('histaminase') group of enzymes (Buffoni, 1966) which have been shown to contain Cu2+, and in some cases pyridoxal phosphate as their prosthetic groups, for example the ox plasma enzyme (Yamada & Yasunobu, 1962b, 1963, the pig plasma enzyme (Blaschko & Buffoni, 1966), the pig kidney intracellular enzyme (Kapeller-Adler & MacFarlane, 1963; Mondovl, Costa, Finazzi-Agrb & Rotilio, 1967a), the pea seedling enzyme (Hill & Mann, 1964), and the enzymes from A. niger (Yamada et al 1965b;Adachi & Yamada, 1969) and Trichosporon sp. (Yamada, Kumagai, Uwajima & Ogata, 1966).…”

Section: Discussionmentioning

confidence: 76%

Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM 1

Eady

Large

1971

Biochemical Journal

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1. An improved procedure is reported for purification of the amine dehydrogenase from methylamine-grown Pseudomonas AM1 which yielded a product homogeneous by sedimentation and disc-electrophoretic analysis, with molecular weight of 133000. 2. The purified enzyme had absorption maxima at 280 and 430nm. On aging, a third peak appeared at 325nm, and the 430nm peak decreased in intensity. This spectrum was independent of pH. 3. Addition of 2.5mm-semicarbazide, phenylhydrazine, hydrazine or hydroxylamine produced modified spectra with maxima respectively at 400, 440, 395 and 425nm. 4. Aerobic addition of methylamine resulted in a bleaching of the 430nm peak and the appearance of a new one at 325nm. This spectral change was retained after removal of the methylamine by dialysis. The original spectrum could be restored on addition of phenazine methosulphate. 5. Addition of borohydride partially inactivated the enzyme and produced spectral changes similar to those observed with methylamine. Pre-treatment with methylamine prevented the inactivation by borohydride. The degree of inactivation could be increased by alternate phenazine methosulphate and borohydride treatments. 6. The addition of methylamine or borohydride each caused shifts in the fluorescence emission maximum from 348 to 380nm. 7. Lineweaver-Burk plots of reciprocal activity against reciprocal concentration of either of the substrates n-butylamine or phenazine methosulphate were consistent with a mechanism that involves interconversion of two free forms of the enzyme by the two substrates. 8. The enzyme, although spectrally modified, was not inactivated by dialysis against diethyldithiocarbamate, and contained about 0.27 g-atom of copper/mol, with small traces of cobalt, iron and zinc. 9. Conventional methods of resolution did not release the prosthetic group. Heat denaturation after treatment of the enzyme with methylamine liberated a yellow chromophore which did not reactivate resolved aspartate aminotransferase, and whose spectral, electrophoretic and fluorescence properties did not agree with any recognizable pyridoxal derivatives. 10. Despite the inconclusive results with the isolated chromophore, the observations on the enzyme suggest that it may contain a pyridoxal derivative bound as a Schiff's base which is converted into the pyridoxamine form on aerobic treatment with methylamine and reconverted into the pyridoxal form with phenazine methosulphate. 11. The copper detected is probably not involved in the enzyme mechanism, since most copper-chelating agents are not inhibitory, and since the enzyme does not react with oxygen.

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Section: Discussionmentioning

confidence: 76%

Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM 1

Eady

Large

1971

Biochemical Journal

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“…Although diamine oxidase was discovered already in 1929 by BEST [1], classified in 1938 by ZELLER [2], highly purified and intensely studied for its biochemical properties by several authors [3][4][5], nothing is certainly known about its physiological or pathophysiological significance.…”

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confidence: 98%

“…Besides kidneys and placenta the gastrointestinal tract contains the highest activities of diamine oxidase in the body of many mammalian species including man [3,4,7,27,28]. Since in this organ system also the highest concentrations of several biogenic amines, such as histamine [29] were found, the small intestine was considered as the most suitable tissue for studying both properties and pathophysiological functions of diamine oxidase.…”

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confidence: 99%

Diamine oxydase in rabbit small intestine: Separation from a soluble monoamine oxidase, properties and pathophysiological significance in intestinal ischemia

et al. 1975

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From all mammals investigated so far only in rabbits diamine oxidase could not be detected in any tissue except the gut. Thus this species was chosen for studying the physiological and pathophysiological function of this enzyme in the gastrointestinal tract. By gel filtration on Sephadex G 50 and G 200 the enzyme was purified 100-fold, separated from a soluble monoamine oxidase, and the properties of the two enzymes were determined. Diamine oxidase from rabbit small intestine deaminated putrecine (Km = 1.3 times 10(-4) M, pH-optimum 6.4-6.9) and histamine (Km = 8 times 10(-5) M, pH-optimum 7.5), but not serotonin, and was inhibited by aminoguanidine, but not by pargyline. Soluble monoamine oxidase from rabbit small intestine catabolized serotonin (Km = 1.8 times 10(-4) M, pH-optimum 8.8) but not putrescine and histamine, and was inhibited by pargyline, but not by aminoguanidine. Based on its properties in vitro intestinal diamine oxidase could inactivate the vasoactive biogenic amine histamine in vivo. To confirm this hypothesis, in rabbits the small intestine was damaged severely by inducing total intestinal ischemia, which occurs as mesenteric infarction also in human subjects and is accompanied by histamine release. Treatment with aminoguanidine and ischemia killed the animals 3-times faster than ischemia alone, which supported our hypothesis on a protective role of intestinal diamine oxidase against histamine.

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“…The reaction has been followed by the measurement of oxygen either manometricly [3,4] or with an oxygen electrode [5]. Procedures have been developed for measuring ammonia [6] and peroxide [7,8]. The aldehyde products from p-dimethylaminomethylbenzylamine [9], p-nitrobenzylamine [10], 1 Current address: Berlin, Penna.…”

Section: ~3mentioning

confidence: 99%

An improved spectrophotometric assay for histamine and diamine oxidase (DAO) activity

Stoner

1985

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Diamlne oxidase or its substrates can be measured using a coupled reaetion with peroxidase and the ehromogen 3-methyl-2-benzothiazolone hydrazone (MBTH) with an appropriate aeeeptor such as 3-(dimethylamino)henzoic acid (DMAB). This method provides a more rapid and sensitive method of measuring histamine than current colorimetrle assays; using this system, histamine was quantltated at eoneentrations of 10 to 400/~mol]l. The Km of DAO was determined to be 2.9 x 10 -5 M, a lower value than previously reported.

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Purification and identification of hog-kidney histaminase

Cited by 45 publications

References 42 publications

Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM 1

Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM 1

Diamine oxydase in rabbit small intestine: Separation from a soluble monoamine oxidase, properties and pathophysiological significance in intestinal ischemia

An improved spectrophotometric assay for histamine and diamine oxidase (DAO) activity

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