scholarly journals Spermidine oxidase in human pregnancy serum. Probable identity with diamine oxidase

1982 ◽  
Vol 201 (1) ◽  
pp. 161-166 ◽  
Author(s):  
W A Gahl ◽  
A M Vale ◽  
H C Pitot
Keyword(s):  
Oxidase Activity ◽  
Diamine Oxidase ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Ph Optimum ◽  
Human Pregnancy ◽  
Diamine Oxidase Activity ◽  
Radioactive Assay ◽  
Spermidine Oxidase ◽  
In Pregnancy

Diamine oxidase was previously measured in human pregnancy serum with putrescine or histamine as substrate. We have now documented the presence of spermidine oxidase activity in pregnancy serum by means of a specific radioactive assay with [14C]spermidine as substrate and Dowex 50 cation-exchange chromatography to separate products from substrate. The apparent Km of a partially purified preparation of this enzyme for spermidine was 10.9 microM and the Ki for aminoguanidine was 0.8 microM. The pH optimum (pH 9.0) and temperature optimum (55 degrees C) were identical with those for diamine oxidase. Spermidine oxidase activity and diamine oxidase activity eluted in a concerted fashion when pregnancy serum was subjected to cadaverine-Sepharose chromatography, gel filtration and ion-exchange chromatography. Spermidine oxidase became detectable in serum during pregnancy in the human approx. 8 weeks after the last menstrual period and increased with gestational age in concert with the increase in diamine oxidase activity, reaching a plateau at 20 weeks of gestation. Foetal-cord serum displayed virtually no activity of either enzyme. A 400-fold-purified preparation of diamine oxidase retained the same diamine oxidase/spermidine oxidase ratio as exhibited by crude pregnancy serum. These data suggest that in pregnancy serum, unlike foetal bovine serum, spermidine oxidase and diamine oxidase activity may be a single enzyme protein.

PP165-MON THE INFLUENCE OF MENSTRUAL CYCLE ON SERUM DIAMINE OXIDASE ACTIVITY IN HEALTHY WOMEN

2011 ◽  
Vol 6 (1) ◽  
pp. 176-177
Author(s):  
Y. Hamada ◽  
Y. Shinohara ◽  
M. Yano ◽  
M. Yamamoto ◽  
M. Yoshio ◽  
...  
Keyword(s):  
Menstrual Cycle ◽  
Oxidase Activity ◽  
Diamine Oxidase ◽  
Healthy Women ◽  
Diamine Oxidase Activity

Intestinal Permeability and Postheparin Plasma Diamine Oxidase Activity in the Prediction of Crohnʼs Disease Relapse

1999 ◽  
Vol 5 (2) ◽  
pp. 85-91 ◽  
Author(s):  
Robert J. Hilsden ◽  
Jon B. Meddings ◽  
James Hardin ◽  
Grant D. Gall ◽  
Lloyd R. Sutherland
Keyword(s):  
Intestinal Permeability ◽  
Oxidase Activity ◽  
Diamine Oxidase ◽  
Disease Relapse ◽  
Diamine Oxidase Activity

Elevated Histaminase (Diamine Oxidase) Activity in Small-Cell Carcinoma of the Lung

1975 ◽  
Vol 293 (25) ◽  
pp. 1286-1290 ◽  
Author(s):  
Stephen B. Baylin ◽  
Martin D. Abeloff ◽  
Kathleen C. Wieman ◽  
J. Walton Tomford ◽  
David S. Ettinger
Keyword(s):  
Cell Carcinoma ◽  
Small Cell Carcinoma ◽  
Oxidase Activity ◽  
Diamine Oxidase ◽  
Small Cell ◽  
Diamine Oxidase Activity

scholarly journals Relationship between postnatal days, serum Cu concentration and plasma diamine oxidase activity in Japanese Black calves

2020 ◽  
Vol 82 (10) ◽  
pp. 1488-1491
Author(s):  
Tatsuya FUKUDA ◽  
Kenji TSUKANO ◽  
Marina OTSUKA ◽  
Yoshiki MURAKAMI ◽  
Yasuyuki KITADE ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Diamine Oxidase ◽  
Diamine Oxidase Activity

Physicochemical properties of a novel α-L-arabinofuranosidase fromRhizomucor pusillusHHT-1

2001 ◽  
Vol 47 (8) ◽  
pp. 767-772 ◽  
Author(s):  
A KM Shofiqur Rahman ◽  
Shinya Kawamura ◽  
Masahiro Hatsu ◽  
M M Hoq ◽  
Kazuhiro Takamizawa
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Gel Filtration ◽  
Hydrolytic Activity ◽  
Exchange Chromatography ◽  
Ph Optimum ◽  
Rhizomucor Pusillus ◽  
Terminal Amino ◽  
Metal Cofactors

The zygomycete fungus Rhizomucor pusillus HHT-1, cultured on L(+)arabinose as a sole carbon source, produced extracellular α-L-arabinofuranosidase. The enzyme was purified by (NH4)2SO4fractionation, gel filtration, and ion exchange chromatography. The molecular mass of this monomeric enzyme was 88 kDa. The native enzyme had a pI of 4.2 and displayed a pH optimum and stability of 4.0 and 7.0–10.0, respectively. The temperature optimum was 65°C, and it was stable up to 70°C. The Kmand Vmaxfor p-nitrophenyl α-L-arabinofuranoside were 0.59 mM and 387 µmol·min–1·mg–1protein, respectively. Activity was not stimulated by metal cofactors. The N-terminal amino acid sequence did not show any similarity to other arabinofuranosidases. Higher hydrolytic activity was recorded with p-nitrophenyl α-L-arabinofuranoside, arabinotriose, and sugar beet arabinan; lower hydrolytic activity was recorded with oat–spelt xylan and arabinogalactan, indicating specificity for the low molecular mass L(+)-arabinose containing oligosaccharides with furanoside configuration.Key words: α-L-arabinofuranosidase, enzyme purification, amino acid sequence, Rhizomucor pusillus.

Regulation of gastric mucosal diamine oxidase activity by gastrin

FEBS Letters ◽  
1992 ◽  
Vol 307 (2) ◽  
pp. 135-138 ◽  
Author(s):  
David M. Hougaard ◽  
Gunnar Houen ◽  
Lars-Inge Larsson
Keyword(s):  
Oxidase Activity ◽  
Diamine Oxidase ◽  
Diamine Oxidase Activity
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