Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens.

Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens. Abstract Text:

M Okada,S Kawashima,K Imahori,

Putrescine oxidase [EC 1.4.3.4], putrescine : oxygen oxidoreductase (deaminating) (flavin-containing), from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens were adsorbed on amine-Sepharose 4B in which one of the terminal amino groups of diamine or triamine was covalently bound to Sepharose 4B leaving the other terminal amino group(s) free. The affinities of these enzymes for the amine-Sepharose 4B increased on increasing the chain length of the methylene groups in the immobilized amines and fell upon addition of the substrate. The affinity of putrescine oxidase modified with 1-ethyl-3-(3-dimethylamino-propyl)-carbodiimide (EDC) was reduced in comparison with that of the native enzyme so far as 1,12-diaminododecane-Sepharose 4B was concerned. From these results, it can be concluded that the interactions between the enzyme and the amine-Sepharose result from specific affinities mediated through the active sites of the enzymes. It is suggested that spermidine dehydrogenase as well as putrescine oxidase has as anionic point and a hydrophobic region in the active site. On the basis of these results, the applicability of the enzyme affinities to purification procedures was examined. When partially purified enzymes were subjected to affinity chromatography, the following results were obtained. Putrescine oxidase gave a purification factor of 40-fold with about 100% recovery on a 1,12-diaminododecane-Sepharose column. In the case of spermidine dehydrogenase, the purification factor and recovery on a 1,8-diaminooctane-Sepharose column were about 1,200-fold and 86%, respectively. By introducing affinity chromatography as a purification step, each enzyme could be purified more simply and with higher recovery.

Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens. Publishing Authors By Initials

M Okada,S Kawashima,K Imahori,

For similar organic chemicals: amines: biogenic amines: biogenic polyamines: putrescine: spermidine research abstracts see: organic chemicals: amines: biogenic amines: biogenic polyamines: putrescine: spermidine research

PUBMED ID PMID:

MEDLINE DATE:

Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 85

Page Numbers: 1225-33

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: May

YEAR: 1979

Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens. Keywords Mesh Terms:

KEYWORDS: Spermidine

MESH TERMS: enzymology

Chemical & Substance for Abstract: Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens. Information

Substance Name: Oxidoreductases Acting on CH-NH Group Do

Registry Number: EC 1.5.-

Grant and Affiliation Information for Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens Related Publications

• A change in circular dichroism due to the binding of guanosine-3-phosphate to ribonuclease T1.
• Affinity labeling of adenine nucleotide-related enzymes with reactive adenine nucleotide analogs. I. Affinity labeling of glyceraldehyde 3-phosphate dehydrogenase and myokinase with a reactive AMP analog.
• Affinity labeling of adenine nucleotide-related enzymes with reactive adenine nucleotide analogs. II. Affinity labeling of phosphoglycerate kinase with a reactive AMP analog.
• CD and fluorescence studies of tRNAPhe from baker's yeast.
• Circular dichroism and conformation of natural and synthetic polynucleotides.
• Conformation of cytidine group in the complex of pancreatic ribonuclease A and cytidine-2'-phosphate.
• Dessociation and reconstitution of colicin E3 and immunity substance complex.
• Difference spectral studies on the interactions between ribonuclease T and its substrate analogues.
• Fluorometric investigation of the local conformation of 16S rRNA in the regions of the 3'- and 5'-ends.
• Fructose-1, 6-bisphosphatase of an extreme thermophile.
• Fructose-diphosphate aldolase of Horseshoe crab (Tachypleus tridentatus).
• Glyceraldehyde 3-phosphate dehydrogenase of Bacillus stearothermophilus. Kinetics and physicochemical studies.
• Glyceraldehyde-3-phosphate dehydrogenase of horseshoe crab (Tachypleus tridentatus).
• Hemodynamic and metabolic changes after carotid endarterectomy in patients with high-degree carotid artery stenosis.
• Hybridization of glyceraldehyde-3-phosphate dehydrogenase in borate.
• Isolation and some properties of glyceraldehyde 3-phosphate dehydrogenase from vegetative cells of Bacillus cereus.
• Phosphoglycerate kinase of Bacillus stearothermophilus.
• Physico-chemical characterization of tyrosyl residues in alpha-chymotrypsinogen and pi-chymotrypsin.
• Physiochemical properties of deoxyribonucleic acid from an extreme thermophile.
• Properties of etiohemoglobin and dimethylprotohemoglobin.
• Protein synthesis in a cell-free system from an extreme thermophile. Effects of preincubation in the cold on polyuridylic acid-dependent polyphenylalanine synthesis at high temperature.
• Purification and characterization of tyrosyl-RNA synthetase from baker's yeast.
• Purification and some properties of DNA-dependent RNA polymerase from an extreme thermophile, Thermus thermophilus HB8.
• Structure of phosphoprotein metabolically active in phosphorylation and dephosphorylation reactions.
• Studies on a thermophilic RNA polymerase which is active only on poly d(A-T) and poly dAdT.
• Studies on an alpha-amylase from a thermophilic bacterium. I. Purification and characterization.
• Studies on phosphoglucomutase from an extreme thermophile, Flavobacterium thermophilum HB8. I. Thermostability and other enzymatic properties.
• Study of circular dichroism of proteins and polypeptides in relation to their backbone and side chain conformations.
• The characterization of newly synthesized RNA in step up cultures of yeast cells.
• The difference in the availabilities of initiation points of phage RNA cistrons in their translation.