Studies on Rat Liver Catalase IV. Heterogeneity of Mitochondrial and Supermatant Catalase*

Higashi, Tokuhiko; Shibata, Yasuo

doi:10.1093/oxfordjournals.jbchem.a128238

Cited by 18 publications

(5 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One component might be catalase or some other hydrogen peroxide destroying system (Mills, 1960), as a linear relationship was noted when large amounts of catalase had been added to the incubations. Catalase activity has been found both in the supernatant and particulate fractions of liver homogenates (Greenfield and Price, 1956;Radhakrishnan and Sarma, 1964;Higashi and Shibata, 1965), but it is apparently not yet established if the soluble catalase is released from the microbodies when the tissue is homogenized (De Duve and Baudhuin, 1966). Previously, evidence was obtained for the formation of an inhibitor at high concentrations of ferrous ion and ascorbate (Lindstedt, 1967).…”

Section: Discussionmentioning

confidence: 99%

Hydroxylation of γ-Butyrobetaine to Carnitine in Rat Liver^*

Lindstedt¹

1967

Biochemistry

113

View full text Add to dashboard Cite

was hydroxylated to carnitine (3-hydroxy-4trimethylaminobutyric acid) by a partially purified soluble protein fraction from rat liver. The reaction, which required molecular oxygen and ferrous ion, was stimulated by a combination of ascorbate and a reduced nicotinamide-adenine dinucleotide phosphate regenerating system, and also by catalase and by liver microsomes. Significant enrichment of tritium in ybutyrobetaine was obtained when [carboxy-14C-2,3-3H]Y-butyrobetaine had been used as substrate, indi-

show abstract

Section: Discussionmentioning

confidence: 99%

Hydroxylation of γ-Butyrobetaine to Carnitine in Rat Liver^*

Lindstedt¹

1967

Biochemistry

113

View full text Add to dashboard Cite

show abstract

“…Several reports on chromatographic and electrophoretic differences between soluble and particlebound catalases have appeared (20,27,28). They can be questioned on the basis that the exposure of the enzyme during fractionation to two different biochemical environments, that of the supernate and that of the particulate fraction, could lead to , and in rats that had received Su-13437 for 3.5 days (filled circles).…”

Section: Catalase In the Supernatementioning

confidence: 99%

Structure, composition, physical properties, and turnover of proliferated peroxisomes. A study of the trophic effects of Su-13437 on rat liver.

Leighton¹,

Coloma²,

Koenig³

1975

The Journal of Cell Biology

161

View full text Add to dashboard Cite

Peroxisome proliferation has been induced with 2-methyl-2-(p-[l,2,3,4-tetrahydro-l-naphthyl]-phenoxy)-propionic acid (Su-13437). DNA, protein, cytochrome oxidase, glucose-6-phosphatase, and acid phosphatase concentrations remain almost constant. Peroxisomal enzyme activities change to approximately 165%, 50% 30% and 0% of the controls for catalase, urate oxidase, L-a-hydroxy acid oxidase, and D-amino acid oxidase, respectively. For catalase the change results from a decrease in particle-bound activity and a fivefold increase in soluble activity. The average diameter of peroxisome sections is 0.58 • 0.15 tzm in controls and 0.73 • 0.25 ~tm after treatment. Therefore, the measured peroxisomal enzymes are highly diluted in proliferated particles.After tissue fractionation, approximately one-half of the normal peroxisomes and all proliferated peroxisomes show matric extraction with ghost formation, but no change in size. In homogenates submitted to mechanical stress, proliferated peroxisomes do not reveal increased fragility; unexpectedly, Su-13437 stabilizes lysosomes. Our results suggest that matrix extraction and increased soluble enzyme activities result from transmembrane passage of peroxisomal proteins.The changes in concentration of peroxisomal oxidases and soluble catalase after Su-13437 allow the calculation of their half-lives. These are the same as those found for total catalase, in normal and treated rats, after allyl isopropyl acetamide: about 1.3 days, a result compatible with peroxisome degradation by autophagy. A sequential increase in liver RNA concentration, [l~C]leucine incorporation into DOC-soluble proteins and into immunoprecipitable catalase, and an increase in liver size and peroxisomal volume per gram liver, characterize the trophic effect of the drug used. In males, Su-13437 is more active than CPIB, another peroxisome proliferation-inducing drug; in females, only Su-13437 is active.Peroxisomes are cell organelles, widely distributed in eucaryotic cells, whose function is partially known only in protists (48) and plants (6,29,59). Their role in animal tissues is not known, in spite of the various physical, morphological, and biochemical analyses to which they have been subjected (2,16,31,42,43). Most of the work has concentrated on rat liver peroxisomes, but their set

show abstract

“…Much of the confusion in regard to the isoenzyme status of catalase may be traced back to the realization that changes in nett surface charge often accompany purification, storage or exposure of this enzyme to oxidizing agents (Thorup & Carpenter, 1962;Heidrich, 1968 ; Morikofer-Zwez et al, 1969). Although catalase had previously been resolved into multiple forms by techniques such as ion-exchange chromatography (Price & Greenfield, 1954; Nishimura, Carson & Kobara, 1964; Higashi & Shibata, 1965), immunoelectrophoresis (Nishimura et al, 1964; Nishimura & Patton, 1966) and acrylamide-gel electrophoresis (Holmes & Masters, 1965), many of these studies were not considered acceptable as definitive evidence for the existence of isoenzymes in the native state because of the possibility of such artifactual changes. In addition, this multiplicity of catalase seemed to stand in contrast to the simple chemical and genetic properties of the enzyme.…”

Section: )mentioning

confidence: 99%

Isoenzymes and Ontogeny

Masters

Holmes

1972

Biological Reviews

View full text Add to dashboard Cite

Summary 1. In this review, representative data on the nature of enzyme multiplicity and the developmental progressions of multiple enzyme forms have been collected, and the significance of this material has been discussed in relation to gene involvement during tissue differentiation. 2. In addition, emphasis has been directed towards the relevance of this onto‐genetic information to a wide variety of biological phenomena, such as the possibilities of metabolic advantage conferred by the distinctive properties and physiological locations of these multiple enzyme forms, the insight into the subunit structure and compositional interrelationships of proteins, the aetiology of disease states, the relationship to hormone action, the extra nuclear specification of enzymes, and the transformations between particulate and soluble enzymes. 3. Three isoenzyme systems in particular have been chosen for the special development of these themes and treated in some detail; lactate dehydrogenase (LDH), aldolase and the esterases. Briefer accounts of the ontogeny of other less‐studied series of multiple enzyme forms have also been included. 4. In relation to LDH, the major findings and conclusions of the pioneering investigators have been outlined, together with the reassessments which have been necessitated by recent studies of LDH ontogeny. It is evident, for example, that the early embryonic form of this enzyme is not necessarily parental as previously thought, and the realization appears to possess wide‐ranging implications in regard to the control of synthesis of the enzymes. An indirect role of oxygen in LDH biosynthesis is indicated together with the independent regulation of the separate genes. 5. Recent developments in the enzymology of preimplantation ova have been discussed. It is noteworthy that the extraordinary levels of LDH activity which have been reported to be associated with these early developmental stages, may arise by extracellular adsorption rather than by an intrinsic synthesis of enzyme. Hence contemporary interest in this area has shifted towards a comprehension of the biochemical significance of the extremely unusual, selective concentrations of extracellular lactate dehydrogenase in the oviduct, the relation of this enzyme to the specialized growth requirements of the ova, and the influences of reproductive hormones on these oviducal isoenzymes. 6. The role of aldolase ontogeny as well as the composition, gene control, and native state of these lysases is also reviewed. This enzyme provides a particular example of the manner in which tissue modification of the catalytic and structural properties of enzymes may influence interpretations of the native state of purified proteins, and in this case, also, the observable microheterogeneity satisfies previous disquietude in regard to the existence of different subunits in the muscle enzyme. 7. The basic developmental importance of aldolase‐C is stressed by the occurrence of this form of the enzyme in the early embryos of many different species. Furthermore, a ...

show abstract

Studies on Rat Liver Catalase IV. Heterogeneity of Mitochondrial and Supermatant Catalase*

Cited by 18 publications

References 0 publications

Hydroxylation of γ-Butyrobetaine to Carnitine in Rat Liver^*

Hydroxylation of γ-Butyrobetaine to Carnitine in Rat Liver^*

Structure, composition, physical properties, and turnover of proliferated peroxisomes. A study of the trophic effects of Su-13437 on rat liver.

Isoenzymes and Ontogeny

Contact Info

Product

Resources

About

Studies on Rat Liver Catalase IV. Heterogeneity of Mitochondrial and Supermatant Catalase*

Cited by 18 publications

References 0 publications

Hydroxylation of γ-Butyrobetaine to Carnitine in Rat Liver*

Hydroxylation of γ-Butyrobetaine to Carnitine in Rat Liver*

Structure, composition, physical properties, and turnover of proliferated peroxisomes. A study of the trophic effects of Su-13437 on rat liver.

Isoenzymes and Ontogeny

Contact Info

Product

Resources

About

Hydroxylation of γ-Butyrobetaine to Carnitine in Rat Liver^*

Hydroxylation of γ-Butyrobetaine to Carnitine in Rat Liver^*