Localization of Enzymes in Mycoplasma.
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Journal: 2006/May - Journal of Bacteriology
ISSN: 0021-9193
PUBMED: 16562057
Abstract:
Pollack, J. D. (University of Connecticut, Storrs), Shmuel Razin, and Robert C. Cleverdon. Localization of enzymes in Mycoplasma. J. Bacteriol. 90:617-622. 1965.-Cells of eight parasitic and two saprophytic Mycoplasma strains were lysed by use of osmotic shock, and the membranes were separated from the soluble fraction by use of differential centrifugation. Cell fractions were tested for reduced nicotinamide adenine dinucleotide (NADH(2)) oxidase, reduced nicotinamide adenine dinucleotide phosphate (NADPH(2)) oxidase, glucose-6-phosphate dehydrogenase, adenosine triphosphatase, ribonuclease, and deoxyribonuclease activities. Adenosine triphosphatase was confined to the membrane fraction of all Mycoplasma strains. The NADH(2) oxidase activity was associated with the membranes of the saprophytic M. laidlawii and with the soluble fraction of the parasitic Mycoplasma strains. NADPH(2) oxidase activity was detected only in the soluble fraction of the parasitic strains. Glusose-6-phosphate dehydrogenase was demonstrated only in the soluble fraction of M. laidlawii. Ribonuclease activity was found usually in both membrane and soluble fractions, but was generally higher in the membrane fraction. In the human and bovine Mycoplasma strains, deoxyribonuclease activity could not be demonstrated in the soluble fraction; in the remaining strains, activity was highest in the soluble fraction. Dissolution of M. laidlawii strain B membranes by sodium deoxycholate significantly increased membrane-NADH(2) oxidase and adenosine triphosphatase activities.
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J Bacteriol 90(3): 617-622
PMID: 16562057

Localization of Enzymes in <em>Mycoplasma</em><sup><a href="#fn1" rid="fn1" class=" fn">1</a></sup>

Abstract

Pollack, J. D. (University of Connecticut, Storrs), Shmuel Razin, and Robert C. Cleverdon. Localization of enzymes in Mycoplasma. J. Bacteriol. 90:617–622. 1965.—Cells of eight parasitic and two saprophytic Mycoplasma strains were lysed by use of osmotic shock, and the membranes were separated from the soluble fraction by use of differential centrifugation. Cell fractions were tested for reduced nicotinamide adenine dinucleotide (NADH2) oxidase, reduced nicotinamide adenine dinucleotide phosphate (NADPH2) oxidase, glucose-6-phosphate dehydrogenase, adenosine triphosphatase, ribonuclease, and deoxyribonuclease activities. Adenosine triphosphatase was confined to the membrane fraction of all Mycoplasma strains. The NADH2 oxidase activity was associated with the membranes of the saprophytic M. laidlawii and with the soluble fraction of the parasitic Mycoplasma strains. NADPH2 oxidase activity was detected only in the soluble fraction of the parasitic strains. Glusose-6-phosphate dehydrogenase was demonstrated only in the soluble fraction of M. laidlawii. Ribonuclease activity was found usually in both membrane and soluble fractions, but was generally higher in the membrane fraction. In the human and bovine Mycoplasma strains, deoxyribonuclease activity could not be demonstrated in the soluble fraction; in the remaining strains, activity was highest in the soluble fraction. Dissolution of M. laidlawii strain B membranes by sodium deoxycholate significantly increased membrane-NADH2 oxidase and adenosine triphosphatase activities.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • BURROUS SE, WOOD WA. Enzyme distribution in membrane, cytoplasm, and nuclear fractions from Pseudomonas fluorescens. J Bacteriol. 1962 Aug;84:364–369.[PMC free article] [PubMed] [Google Scholar]
  • DOI RH, HALVORSON H. Mechanism of dipicolinic acid stimulation of the soluble reduced diphosphopyridine nucleotide oxidase of spores. J Bacteriol. 1961 Apr;81:642–648.[PMC free article] [PubMed] [Google Scholar]
  • DOLIN MI. Oxidation of reduced diphosphopyridine nucleotide by Clostridium perfringens. I. Relation of peroxide to the overall reaction. J Bacteriol. 1959 Apr;77(4):383–392.[PMC free article] [PubMed] [Google Scholar]
  • DOLIN MI. Oxidation of reduced diphosphopyridine nucleotide by Clostridium perfringens. II. Purification of the oxidase: relation to cytochrome c reductase. J Bacteriol. 1959 Apr;77(4):393–402.[PMC free article] [PubMed] [Google Scholar]
  • DOWNEY RJ. VITAMIN K-MEDIATED ELECTRON TRANSFER IN BACILLUS SUBTILIS. J Bacteriol. 1964 Oct;88:904–911.[PMC free article] [PubMed] [Google Scholar]
  • DRAPEAU GR, MACLEOD RA. NUTRITION AND METABOLISM OF MARINE BACTERIA. XII. ION ACTIVATION OF ADENOSINE TRIPHOSPHATASE IN MEMBRANES OF MARINE BACTERIAL CELLS. J Bacteriol. 1963 Jun;85:1413–1419.[PMC free article] [PubMed] [Google Scholar]
  • DWORKIN M, NIEDERPRUEM DJ. ELECTRON TRANSPORT SYSTEM IN VEGETATIVE CELLS AND MICROCYSTS OF MYXOCOCCUS XANTHUS. J Bacteriol. 1964 Feb;87:316–322.[PMC free article] [PubMed] [Google Scholar]
  • GILBY AR, FEW AV. Lysis of protoplasts of Micrococcus lysodeikticus by ionic detergents. J Gen Microbiol. 1960 Aug;23:19–26. [PubMed] [Google Scholar]
  • HUGHES DE. The bacterial cytoplasmic membrane. J Gen Microbiol. 1962 Sep;29:39–46. [PubMed] [Google Scholar]
  • LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  • MCDONALD IJ. LOCATION OF PROTEINASE, PEPTIDASE, CATALASE, AND NADH OXIDASE IN CELLS OF STAPHYLOCOCCUS LACTIS. Can J Microbiol. 1964 Apr;10:197–200. [PubMed] [Google Scholar]
  • MITCHELL P. Metabolism, transport, and morphogenesis: which drives which? J Gen Microbiol. 1962 Sep;29:25–37. [PubMed] [Google Scholar]
  • Munro AJ, Jackson RJ, Korner A. Studies on the nature of polysomes. Biochem J. 1964 Aug;92(2):289–299.[PMC free article] [PubMed] [Google Scholar]
  • PEPPER RE, COSTILOW RN. ELECTRON TRANSPORT IN BACILLUS POPILLIAE. J Bacteriol. 1965 Feb;89:271–276.[PMC free article] [PubMed] [Google Scholar]
  • Pollack JD, Razin S, Pollack ME, Cleverdon RC. Fractionation of mycoplasma cells for enzyme localization. Life Sci. 1965 May;4(9):973–977. [PubMed] [Google Scholar]
  • RAZIN S. OSMOTIC LYSIS OF MYCOPLASMA. J Gen Microbiol. 1963 Dec;33:471–475. [PubMed] [Google Scholar]
  • RAZIN S. FACTORS INFLUENCING OSMOTIC FRAGILITY OF MYCOPLASMA. J Gen Microbiol. 1964 Sep;36:451–459. [PubMed] [Google Scholar]
  • RAZIN S, ARGAMAN M, AVIGAN J. CHEMICAL COMPOSITION OF MYCOPLASMA CELLS AND MEMBRANES. J Gen Microbiol. 1963 Dec;33:477–487. [PubMed] [Google Scholar]
  • RAZIN S, KNIGHT BC. The effects of ribonucleic acid and deoxyribonucleic acid on the growth of Myeoplasma. J Gen Microbiol. 1960 Apr;22:504–519. [PubMed] [Google Scholar]
  • RAZIN S, KNYSZYNSKI A, LIFSHITZ Y. NUCLEASES OF MYCOPLASMA. J Gen Microbiol. 1964 Aug;36:323–332. [PubMed] [Google Scholar]
  • ROBRISH SA, MARR AG. Location of enzymes in Azotobacteragilis. J Bacteriol. 1962 Jan;83:158–168.[PMC free article] [PubMed] [Google Scholar]
  • ROTHBLAT GH, SMITH PF. Nonsaponifiable lipids of representative pleuropneumonia-like organisms. J Bacteriol. 1961 Oct;82:479–491.[PMC free article] [PubMed] [Google Scholar]
  • WEIBULL C, BECKMAN H, BERGSTROM L. Localization of enzymes in Bacillus megaterium, strain M. J Gen Microbiol. 1959 Jun;20(3):519–531. [PubMed] [Google Scholar]
  • WEIBULL C, GREENWALT JW, LOW H. The hydrolysis of adenosine triphosphate by cell fractions of Bacillus megaterium. I. Localization and general characteristics of the enzymic activities. J Biol Chem. 1962 Mar;237:847–852. [PubMed] [Google Scholar]
  • WHITE DC, SMITH L. LOCALIZATION OF THE ENZYMES THAT CATALYZE HYDROGEN AND ELECTRON TRANSPORT IN HEMOPHILUS PARAINFLUENZAE AND THE NATURE OF THE RESPIRATORY CHAIN SYSTEM. J Biol Chem. 1964 Nov;239:3956–3963. [PubMed] [Google Scholar]
Department of Bacteriology, University of Connecticut, Storrs, Connecticut
Recipient of a National Science Foundation Senior Foreign Scientist Fellowship; on leave from the Hebrew University, Jerusalem, Israel.
Deceased 9 March 1965.
Contribution no. 117 of the Institute of Cellular Biology, University of Connecticut.
Copyright notice
Abstract
Pollack, J. D. (University of Connecticut, Storrs), Shmuel Razin, and Robert C. Cleverdon. Localization of enzymes in Mycoplasma. J. Bacteriol. 90:617–622. 1965.—Cells of eight parasitic and two saprophytic Mycoplasma strains were lysed by use of osmotic shock, and the membranes were separated from the soluble fraction by use of differential centrifugation. Cell fractions were tested for reduced nicotinamide adenine dinucleotide (NADH2) oxidase, reduced nicotinamide adenine dinucleotide phosphate (NADPH2) oxidase, glucose-6-phosphate dehydrogenase, adenosine triphosphatase, ribonuclease, and deoxyribonuclease activities. Adenosine triphosphatase was confined to the membrane fraction of all Mycoplasma strains. The NADH2 oxidase activity was associated with the membranes of the saprophytic M. laidlawii and with the soluble fraction of the parasitic Mycoplasma strains. NADPH2 oxidase activity was detected only in the soluble fraction of the parasitic strains. Glusose-6-phosphate dehydrogenase was demonstrated only in the soluble fraction of M. laidlawii. Ribonuclease activity was found usually in both membrane and soluble fractions, but was generally higher in the membrane fraction. In the human and bovine Mycoplasma strains, deoxyribonuclease activity could not be demonstrated in the soluble fraction; in the remaining strains, activity was highest in the soluble fraction. Dissolution of M. laidlawii strain B membranes by sodium deoxycholate significantly increased membrane-NADH2 oxidase and adenosine triphosphatase activities.
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