Purification and identification of hog-kidney histaminase

Kapeller-Adler, Regine; MacFarlane, H.

doi:10.1016/0006-3002(63)91865-1

Cited by 10 publications

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“…On the other hand, Kapeller-Adler (10)(11) reported that DAO and histaminase were different enzymes, since her histaminase preparation purified from hog kidney oxidized histamine but not cadaverine.…”

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confidence: 99%

Enzymic Properties of Diamine Oxidase From Hog Kidney

Suetsugu

1974

Jpn.J.Pharmacol

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Abstract-DAO was partially purified from hog kidney by a procedure involving differential centrifugation, heat treatment and ammonium sulfate fractionation.The enzymic properties of partially purified DAO were studied with cadaverine and hista mine as substrates and the following results were obtained.The specific activities of hog kidney DAO at the final step of purification were 183-fold and 125-fold those of the crude homogenate with histamine and cadaverine, respectively, as substrates. With cadaverine and histamine the pS maxima values were 3×10^-3 M and 1×10^-3 M and the pH optima were 7.1 and 6.5, respectively. All the diamines tested, (i.e. cadaverine, putrescine, hexamethylenediamine, histamine, ethylenediamine and agma tine) were oxidized with this enzyme, while monoamine, (i.e. tyramine, benzylamine, serotonin, β-phenylethylamine, n-amylamine and n-propylamine) were not. DAO activity was inhibited by aminoguanidine, hydroxylamine, MPH and semicarbazide. The inhibitory effects were similar when either cadaverine or histamine was used as substrate. SH-reagents, such as PCMB and iodoacetoamide, did not affect DAO activity, but various metal ions, such as CuCl, Cu(NO₃)₂, Zn(NO₃)₂, AICl₃ and Fe (NO₃)₃ were inhibitory. The inhibitory effect of AgNO₃ on DAO activity differed greatly, when using cadaverine and histamine as substrates. The temperature-in -activation curves of DAO measured with cadaverine and with histamine were different.There have been reports on diamine oxidase (DAO) (E.C. 1.4.3.6. diamine: oxygen oxydoreductase (deaminating)), which catalyzes the oxidation of cadaverine, putrescine and agmatine, and histaminase which catalyzes the oxidation of histamine. Since the substrate specificities of DAO and histaminase are very similar (1-6), Zeller called both enzymes DAO. Goryachenkova (7) and Leloir (8) also suggested that DAO and hista minase were the same enzyme because they could not be separated by electrophoresis .Mondovi et al. (9) also stated that these two enzymes were identical since during purifica tion the ratio of the activities in oxidation of cadaverine and histamine remained almost the same. On the other hand, Kapeller-Adler (10-11) reported that DAO and histaminase were different enzymes, since her histaminase preparation purified from hog kidney oxidized histamine but not cadaverine.Thus although there have been many investigations on the possible identity of these two enzymes, the problem has yet to be clarified. In the present work the amine oxidase was partially purified from hog kidney, and the properties were studied using cadaverine and histamine as substrates.

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confidence: 99%

Enzymic Properties of Diamine Oxidase From Hog Kidney

Suetsugu

1974

Jpn.J.Pharmacol

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“…To determine whether chlorpromazine blocked cortisone induced acid secretion specifically by the inhibition of imidazole-N-methyltransferase or non-specifically by one of its many actions, the effect of another inhibitor of imidazole-N-methyltransferase, 1,4 methylhistamine (Kapeller-Adler & MacFarlaine, 1963;Haverback, Sturbin & Dyce, 1965) was also investigated in conjunction with cortisone. Guinea-pigs were injected with 1,4 methylhistamine 1 mg/kg intraperitoneally immediately following pyloric ligation, or cortisone (see Methods) or both agents in conjunction.…”

Section: Effect Of 14 Methylhistamine On Cortisone Induced Acid Hypementioning

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The possible role of histamine in the cortisone induced gastric acid hypersecretion of the guinea‐pig

Heisler

Kovács

1969

British J Pharmacology

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1. The effects of cortisone treatment combined with agents influencing histamine metabolism were studied on the free and total acid output in pylorus ligated guinea-pigs. 2. It was found that reduction in the synthesis of histamine produced by the administration of a-methylDOPA significantly inhibited the acid response to cortisone. 3. Enhancement of the oxidative deamination of histamine brought about by the administration of diamine oxidase or heparin inhibited cortisone induced acid hypersecretion significantly. 4. Inhibition of the oxidative deamination of histamine tby aminoguanidine and iproniazid resulted in a significant increase of the cortisone induced acid hypersecretory response. 5. Inhibition of the methylation of histamine by chlorpromazine or 1,4-methylhistamine inhibited the cortisone induced hypersecretory response significantly. 6. Studies with labelled histamine indicated that cortisone increases the sequestration of histamine to the stomach.It has been reported by Heisler & Kovacs (1967) that administration of cortisone to guinea-pigs resulted in a decrease in gastric histamine content, while gastric acid secretory activity was increased. The results suggested that an interrelationship between cortisone treatment, gastric histamine release and acid secretion might be the underlying sequence of events in the cortisone induced secretory process.Consequently, studies were designed to suppress the synthesis and enhance or suppress the inactivation of endogenous histamine and to test the effect of these pharmacological alterations on the cortisone induced gastric secretory response. The results presented here suggest that in the guinea-pig cortisone induced acid hypersecretion might be mediated by histamine.

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“…This suggestion was based on the fact th at many substances known to inhibit pyridoxal enzymes are inhibitors of these oxidases. More recently, the earlier suggestions have received some support from spectroscopic and fluorimetric observations on histaminase and other enzymes of this group (Yamada & Yasunobu 1963;Kapeller-Adler & McFarlane 1963;Mondovi, Rotilio, Costa, Finazzi & Scioscia-Santoro 1964). However, it has not been possible so far to isolate the prosthetic group of these enzymes.…”

Section: Introductionmentioning

confidence: 99%

Pyridoxal phosphate as a constituent of the histaminase (benzylamine oxidase) of pig plasma

Blaschko

Buffoni

1965

Proc. R. Soc. Lond. B.

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The histaminase (‘benzylamine oxidase’) of pig plasma has recently been crystallized and a description is given of some of the physical and chemical properties of the pure preparation of the oxidase. The fluorescence of the enzyme is typical of a protein containing tryptophan. The phosphorus content is about four atoms per molecule. On enzymic hydrolysis a product has been obtained that has the fluorescence properties of a pyridoxal protein. This product gave rise on acid hydrolysis to material capable of activating the L-tyrosine apodecarboxylase of Streptococcus faecalis R in the presence of adenosine triphosphate, indicating that pyridoxal was set free in the hydrolysis. Acid hydrolysis of a solution of the crystalline enzyme and subsequent treatment with urea yielded diffusible material with the spectroscopic and fluorescence properties of pyridoxal. Using the bacterial apodecarboxylase, traces of pyridoxal phosphate and larger amounts of free pyridoxal were shown to be present. It was calculated that about 3 or 4 moles of pyridoxal were present per mole of enzyme. Together with the phosphate estimations, these observations lead to the conclusion that the oxidase contains 3 or 4 moles of pyridoxal phosphate per mole. Observations on rats maintained on a diet deficient in vitamin B 6 are in agreement with these conclusions.

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Purification and identification of hog-kidney histaminase

Cited by 10 publications

References 0 publications

Enzymic Properties of Diamine Oxidase From Hog Kidney

Enzymic Properties of Diamine Oxidase From Hog Kidney

The possible role of histamine in the cortisone induced gastric acid hypersecretion of the guinea‐pig

Pyridoxal phosphate as a constituent of the histaminase (benzylamine oxidase) of pig plasma

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