Abstract
The nucleoids of microbodies of rat liver cells were isolated in a highly homogeneous and pure state, by treating the microbody-rich fraction, prepared from 10% polyvinylpyrrolidone-0.25 M sucrose homogenate, with Triton X-100. Three treatments with 0.1% detergent were enough to render the nucleoids free from contamination with mitochondria, microsomes, lysosomes, and intact microbodies. Electron microscopically, the nucleoids were found to consist of parallel bundles of highly dense hollow tubules, the outer and inner diameters of which are approximately 150 and 50 A, respectively. Ten tubules are arranged around a longitudinal space 190 x 200 A in width. The nucleoids thus show a honeycomb appearance in the cross-plane and a parallel-packed structure in the longitudinal plane. Biochemically, the nucleoids were found to bear only urate oxidase among probably microbody-enzymes, and they might be the only cytoplasmic particles of rat liver cells in which the enzyme locates. Urate oxidase activity, on a unit protein basis, of the nucleoid preparation is approximately 380 times as high as that of the whole homogenate, and is almost comparable with that of a commercial type I enzyme preparation. No enzymes of mitochondrial, microsomal, and lysosomal origins were detected in the nucleoids. The fine structure of the nucleoids is described in detail, and a probable schematic diagram is presented.
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- ADAMS D. H., BURGESS E. A. Some factors affecting the permeability of large-granule membranes to mouse-liver catalase in vitro. Biochem J. 1960 Nov;77:247–252. doi: 10.1042/bj0770247. [DOI] [PMC free article] [PubMed] [Google Scholar]
- ADAMS D. H. The mechanism of the liver catalase depressing action of tumours in mice. Br J Cancer. 1950 Jun;4(2):183–195. doi: 10.1038/bjc.1950.18. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BERNHARD W., ROUILLER C. Microbodies and the problem of mitochondrial regeneration in liver cells. J Biophys Biochem Cytol. 1956 Jul 25;2(4 Suppl):355–360. doi: 10.1083/jcb.2.4.355. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Baudhuin P., Beaufay H., De Duve C. Combined biochemical and morphological study of particulate fractions from rat liver. Analysis of preparations enriched in lysosomes or in particles containing urate oxidase, D-amino acid oxidase, and catalase. J Cell Biol. 1965 Jul;26(1):219–243. doi: 10.1083/jcb.26.1.219. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DE DUVE C., BEAUFAY H., JACQUES P., RAHMAN-LI Y., SELLINGER O. Z., WATTIAUX R., DE CONINCK S. Intracellular localization of catalase and of some oxidases in rat liver. Biochim Biophys Acta. 1960 May 6;40:186–187. doi: 10.1016/0006-3002(60)91338-x. [DOI] [PubMed] [Google Scholar]
- ENDAHL B. R., KOCHAKIAN C. D. Role of castration and androgens in D-amino acid oxidase activity of tissues. Am J Physiol. 1956 May;185(2):250–256. doi: 10.1152/ajplegacy.1956.185.2.250. [DOI] [PubMed] [Google Scholar]
- ESSNER E., NOVIKOFF A. B. Localization of acid phosphatase activity in hepatic lysosomes by means of electron microscopy. J Biophys Biochem Cytol. 1961 Apr;9:773–784. doi: 10.1083/jcb.9.4.773. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GREENFIELD R. E., PRICE V. E. Liver catalase. III. Isolation of catalase from mitochondrial fractions of polyvinylpyrrolidonesucrose homogenates. J Biol Chem. 1956 Jun;220(2):607–618. [PubMed] [Google Scholar]
- HRUBAN Z., SWIFT H. URICASE: LOCALIZATION IN HEPATIC MICROBODIES. Science. 1964 Dec 4;146(3649):1316–1318. doi: 10.1126/science.146.3649.1316. [DOI] [PubMed] [Google Scholar]
- NOBUNAGA M. [Studies on beta-glucuronidase. II. Clinical application of the assay method of beta-glucuronidase activity using p-nitrophenylglucuronide as the substrate. III. The significance of the serum beta-glucuronidase activity in patients with liver diseases, with special references to its relation with the serum transaminase activity, and to its characteristic behavior in cholangiolitic hepatitis]. Fukuoka Igaku Zasshi. 1961 Apr 25;52:300–311. [PubMed] [Google Scholar]
- NOVIKOFF A. B., ESSNER E. The liver cell. Some new approaches to its study. Am J Med. 1960 Jul;29:102–131. doi: 10.1016/0002-9343(60)90011-5. [DOI] [PubMed] [Google Scholar]