Steroid regulation of kidney histidine decarboxylase and ornithine decarboxylase levels in mouse kidney: Effects of the mutation testicular feminization,

1988 ◽  
Vol 90 (1) ◽  
pp. 221-225 ◽  
Author(s):  
Richard J. Middleton ◽  
Grahame Bulfield
Keyword(s):  
Ornithine Decarboxylase ◽  
Histidine Decarboxylase ◽  
Mouse Kidney ◽  
Testicular Feminization ◽  
Steroid Regulation

Effects of phorbol ester and dexamethasone treatment on histidine decarboxylase and ornithine decarboxylase in basophilic cells

2001 ◽  
Vol 61 (9) ◽  
pp. 1101-1106 ◽  
Author(s):  
Ignacio Fajardo ◽  
Jose L Urdiales ◽  
Miguel A Medina ◽  
Francisca Sanchez-Jimenez
Keyword(s):  
Ornithine Decarboxylase ◽  
Phorbol Ester ◽  
Histidine Decarboxylase ◽  
Dexamethasone Treatment

Heterogenous expression of ornithine decarboxylase gene in the proximal tubule of the mouse kidney following testosterone treatment

1993 ◽  
Vol 100 (5) ◽  
pp. 325-330 ◽  
Author(s):  
Noriyuki Koibuchi ◽  
Shigeru Matsuzaki ◽  
Mikako Sakai ◽  
Hideki Ohtake ◽  
Sadao Yamaoka
Keyword(s):  
Proximal Tubule ◽  
Ornithine Decarboxylase ◽  
Mouse Kidney ◽  
Testosterone Treatment

Investigation of structure and rate of synthesis of ornithine decarboxylase protein in mouse kidney

Biochemistry ◽  
1984 ◽  
Vol 23 (16) ◽  
pp. 3777-3783 ◽  
Author(s):  
Lo Persson ◽  
James E. Seely ◽  
Anthony E. Pegg
Keyword(s):  
Ornithine Decarboxylase ◽  
Mouse Kidney

scholarly journals Studies of mammalian ornithine decarboxylase using a monoclonal antibody

1984 ◽  
Vol 217 (1) ◽  
pp. 123-128 ◽  
Author(s):  
A E Pegg ◽  
J E Seely ◽  
L Persson ◽  
M Herlyn ◽  
K Ponsell ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Ornithine Decarboxylase ◽  
Mouse Kidney ◽  
Immunoglobulin M ◽  
Active Enzyme ◽  
Sodium Thiocyanate ◽  
Immunoaffinity Column ◽  
Rapid Turnover ◽  
Cytosolic Protein

A monoclonal antibody of the immunoglobulin M class was produced against mouse kidney ornithine decarboxylase. Screening for the antibody was carried out using alpha-difluoromethyl[5-3H]ornithine-labelled ornithine decarboxylase. The antibody reacted with this antigen and with native ornithine decarboxylase. The antibody attached to Sepharose could be used to form an immunoaffinity column that retained mammalian ornithine decarboxylase. The active enzyme could then be eluted in a highly purified form by 1.0M-sodium thiocyanate. The monoclonal antibody could also be used to precipitate labelled ornithine decarboxylase from homogenates of kidneys from androgen-treated mice given [35S]methionine. Only one band, corresponding to Mr of about 55000, was observed. The extensive labelling of this band is consistent with the rapid turnover of ornithine decarboxylase protein, since this enzyme represents only about 1 part in 10000 of the cytosolic protein.

Ornithine decarboxylase in rat small intestine: stimulation with food or insulin

1976 ◽  
Vol 231 (5) ◽  
pp. 1557-1561 ◽  
Author(s):  
DV Maudsley ◽  
J Leif ◽  
Y Kobayashi
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Ornithine Decarboxylase ◽  
Diamine Oxidase ◽  
Actinomycin D ◽  
Histidine Decarboxylase ◽  
Decarboxylase Activity ◽  
Adenosylmethionine Decarboxylase ◽  
Diamine Oxidase Activity ◽  
Similarities And Differences

Ornithine decarboxylase in the small intestine of starved rats was stimulated 3- to 10-fold by refeeding or administration of insulin. A peak is observed 3-5 h following treatment after which the enzyme activity rapidly declines. The rise in ornithine decarboxylase is reduced by actinomycin D or cycloheximide. The increase in enzyme activity occurs mainly in the duodenum and jejunum with less than a twofold change being observed in the ileum. A small (twofold) increase in S-adenosylmethionine decarboxylase activity in the small intestine was observed after food, but there was no change in diamine oxidase activity. Whereas pentagastrin and metiamide administration markedly stimulated histidine decarbosylase in the gastric mucosa, no consistent effect of these agents on ornithine decarboxylase in the small intestine was observed. The similarities and differences between histidine decarboxylase and ornithine decarboxylase are discussed.

scholarly journals Purification and characterization of histidine decarboxylase from mouse kidney

1986 ◽  
Vol 234 (2) ◽  
pp. 349-354 ◽  
Author(s):  
S A M Martin ◽  
J O Bishop
Keyword(s):  
Column Chromatography ◽  
Gel Electrophoresis ◽  
Histidine Decarboxylase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Mouse Kidney ◽  
Purification Procedure ◽  
Purification And Characterization ◽  
A Subunit

Histidine decarboxylase was purified 800-fold from the kidneys of thyroxine-treated mice. The purification procedure included precipitation of protein from a crude supernatant after heating it to 55 degrees C at pH 5.5, fractionation with (NH4)2SO4, phosphocellulose column chromatography, chromatofocusing, DEAE-Sepharose column chromatography, gel filtration on Sephacryl S-300 and preparative polyacrylamide-gel electrophoresis. The native enzyme had an estimated Mr of 113 000. The protein was analysed in SDS/10%-polyacrylamide gels and formed a single band corresponding to a subunit Mr of 55 000, indicating that it is a dimer. Three forms of the enzyme were resolved on isoelectrofocusing gels, with pI 5.3, 5.5 and 5.7.

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