NOTE: Free essay sample provided on this page should be used for references or sample purposes only. The sample essay is available to anyone, so any direct quoting without mentioning the source will be considered plagiarism by schools, colleges and universities that use plagiarism detection software. To get a completely brand-new, plagiarism-free essay, please use our essay writing service.
One click instant price quote
Several rare electrophoretic variants of red cell catalase were identified by Baur (1963). Nance et al. (1968) also described electrophoretic variants. Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988). Wieacker et al. (1980) assigned a gene for catalase to 11 p by study of man-mouse cell hybrid clones. In the hybrid cells, detection of human catalase was precluded by the complexity of the electrophoretic patterns resulting from interference by a catalase-modifying enzyme activity. Therefore, a specific anti human antibody was used in conjunction with electrophoresis.
In mouse, catalase is not synthetic to the beta-globin cluster or to LDH-A. Junien et al. (1980) investigated catalase gene dosage effects in a case of 11 p 13 deletion, a case of trisomy of all of 11 p except 11 p 13, and a case of trisomy 11 p 13. The results were consistent with assignment of the catalase locus to 11 p 13 and its linkage with the WAGR complex (194070). Assay of catalase activity should be useful in identifying those cases of presumed new mutation aniridia that have a risk of Wilms tumor or gonadoblastoma, even in the absence of visible chromosomal deletion. In karyotypically normal patients with aniridia, Wilms tumor, or the combination of the two, Ferrell and Riccardi (1981) found normal catalase levels.
Niikawa et al. (1982) confirmed the close linkage of catalase to the gene of the WAGR complex by demonstrating low levels of catalase activity in the erythrocytes of 2 unrelated patients with the WAGR syndrome and small deletions in 11 p. From the study of dosage in 2 unrelated patients with an interstitial deletion involving 11 p 13, Narahara et al. (1984) concluded that both the catalase locus and the WAGR locus are situated in the chromosome segment 11 p 1306 -p 1305, with catalase distal to WAGR. Boyd et al. (1986) described a catalase RFLP with 2 different enzymes and used these polymorphisms to exclude deletion of the catalase gene in patients with sporadic aniridia, including one who was known to have a deletion and another suspected of having a deletion. Mannens et al. (1987) found deletion of the catalase locus in 6 of 9 patients with aniridia (AN 2; 106210). One of these catalase-deficient aniridia patients had a normal karyotype. No catalase deletion could be demonstrated in 7 Wilms tumors.
By classic linkage studies using Rflp's of the several genes as markers, Kittur et al. (1985) derived the following sequence of loci: cen-CAT -- 16 cM-CALC -- 8 cM-PTH-per, with the interval between CAT and PTH estimated at 26 cM. Differences in molecular weight of enzymes in different tissues is not proof that the enzymes are coded by different genes because tissue-specific variations in transcription or in post translational processing may occur. For example, catalase of red cells and that of liver are of different molecular weight, but from other evidence both are coded by the single gene located on 11 p. Quan et al. (1986) found that the CAT gene is 34 kb long and split into 13 exons.
Bell et al. (1986) gave the cDNA sequence for human kidney catalase. The coding region had 1, 581 base pairs. Acatalasia was first discovered in Japan by Takahara, an otolaryngologist who found that in cases of progressive oral gangrene, hydrogen peroxide applied to the ulcerated areas did not froth in the usual manner (Takahara and Miyamoto, 1948). Heterozygotes have an intermediate level of catalase in the blood. The frequency of the gene, although relatively high in Japan, is variable. The frequency of heterozygote's is 0. 09 408852 n Hiroshima and Nagasaki but is of the order of 1. 4 408852 n other parts of Japan (Hamilton et al. , 1961).
Acatalasia has been detected in Switzerland (Aebi et al. , 1962) and in Israel (Szeinberg et al. , 1963). In the Swiss and the Israelis, the homozygote's showed some residual catalase activity suggesting that this may be a different mutation from that responsible for the Japanese disease in which catalase activity is zero and no cross-reacting material has been identified. Hamilton and Neel (1963) presented evidence that at least 2 forms of acatalasia exist in Japan. In an extensive kindred with acatalasia in 2 sibship's, heterozygote's showed catalase values overlapping with the normal.
Ogata (1991) compared the properties of residual catalase in the Japanese and Swiss forms of the disease and in the mutant mouse. Hypocatalasia has also been found in the guinea pig, dog, and domestic fowl (see review by Lush, 1966). Shibata et al. (1967) found that an immunologically reactive but enzymatically inactive protein about one-sixth the size of active catalase is present in red cells of acatalasemic's. In the acatalasemic mouse, Shaffer and Preston (1990) demonstrated that a CAG (glutamine) -to-CAT (histidine) trans version in the third position of codon 11 was responsible for the deficiency.
Allelic Variants: . 0001 ACATALASEMIA, JAPANESE TYPE CAT, IVS 4, G-A, + 5 By sequencing the CAT gene for all exons, exon / intron junctions, and 5 -prime and 3 -prime flanking regions in a case of the Japanese type of acatalasemia, Wen et al. (1990) concluded that the genetic disorder resulted from a splicing mutation, namely, a G-to-A substitution at the fifth position of intron 4. In studies using chimeric genes constructed from the normal or mutant CAT gene and a part of the alpha-globin gene, Wen et al. (1990) showed that when the mutant gene construct was introduced into COS- 7 cells, abnormal splicing occurred. The same splice site mutation was found in the genomic DNA of another unrelated acatalasemic person. Kishimoto et al. (1992) found the same mutation in 2 other unrelated Japanese patients and suggested that only a single mutated allele had spread in the Japanese population. See Also: Aebi et al. (1964); Aebi and Suter (1972); Agar et al. (1986); Feinstein et al. (1966); Kidd et al. (1987); Matsubara et al. (1967); Matsunaga et al. (1985); Quan et al. (1985); Schroeder and Saunders (1987) References: 1. Aebi, H. ; Baggiolini, M. ; Deals, B. ; Later, E. ; Sutter, H. ; Michael, A. ; Frei, J. : Observations in two Swiss families with acatalasia.
Enzym. Biol. Clin. 4: 121 - 151, 1964. 2. Aebi, H. ; Genet, F. ; Richterich, R. ; Suter, H. ; Butler, R. ; Frei, J. ; Marti, H. R. : Observations in two Swiss families with acatalasia.
Enzym. Biol. Clin. 2: 1 - 22, 1962. 3. Aebi, H. ; Suter, H. : Acatalasia.
In: Stanbury, J. B. ; Wyngaarden, J. B. ; Fredrickson, D. S. : The Metabolic Basis of Inherited Disease. New York: McGraw-Hill (pub. ) (3 rd ed. ): 1972.
Pp. 1710 - 1729. 4. Agar, N. S. ; Sadrzadeh, S. M. H. ; Hallway, P. E. ; Eaton, J.
W. : Erythrocyte catalase: a somatic oxidant defense? . J. Clin. Invest. 77: 319 - 321, 1986. 5. Baur, E. W. : Catalase abnormality in a Caucasian family in the United States.
Science 140: 816 - 817, 1963. 6. Bell, G. I. ; Najarian, R. C. ; Mullenbach, G. T. ; Halle well, R. A. : cDNA sequence coding for human kidney catalase.
Nucleic Acids Res. 14: 5561 - 5562, 1986. 7. Boyd, P. ; van Heyningen, V. ; Sea wright, A. ; Feet, G. ; Hastie, N. : Use of catalase polymorphisms in the study of sporadic aniridia. Hum. Genet. 73: 171 - 174, 1986. 8. Feinstein, R. N. ; Howard, J.
B. ; Braun, J. T. ; Seaholm, J. E. : Acatalasemic and hypocatalasemic mouse mutants. Genetics 53: 923 - 933, 1966. 9.
Ferrell, R. E. ; Riccardi, V. M. : Catalase levels in patients with aniridia and-or Wilms' tumor: utility and limitations. Cytogenet.
Cell Genet. 31: 120 - 123, 1981. 10. Hamilton, H. B. ; Neel, J. V. : Genetic heterogeneity in human acatalasia. Am.
J. Hum. Genet. 15: 408 - 419, 1963. 11. Hamilton, H. B. ; Neel, J.
V. ; Kobara, T. Y. ; Ozaki, K. : The frequency in Japan of carriers of the rare 'recessive' gene causing acatalasemia. J. Clin. Invest. 40: 2199 - 2208, 1961. 12.
Junien, C. ; Turleau, C. ; de Grouchy, J. ; Said, R. ; Restore, M. -O. ; Tenconi, R. ; Duties, J. L. : Regional assignment of catalase (CAT) gene to band 11 p 13: association with the aniridia-Wilms' tumor-gonadoblastoma (WAGR) complex. Ann. Genet. 23: 165 - 168, 1980. 13. Kidd, J. R. ; Castiglione, C.
M. ; Pakstis, A. J. ; Kidd, K. K. : The anonymous RFLP locus D 11 S 16 is tightly linked to catalase on 11 p. Cytogenet.
Cell Genet. 45: 63 - 64, 1987. 14. Kishimoto, Y. ; Murakami, Y. ; Hayashi, K. ; Takahara, S. ; Sugimura, T. ; Sekiya, T. : Detection of a common mutation of the catalase gene in Japanese acatalasemic patients. Hum. Genet. 88: 487 - 490, 1992. 15. Kittur, S. D. ; Happened, J.
W. M. ; Antonarakis, S. E. ; Daniels, J. D. J. ; Meyers, D. A. ; Maestro, N.
E. ; Jansen, M. ; Korneluk, R. G. ; Nelson, B. D. ; Kazazian, H. H. , Jr. : Linkage map of the short arm of human chromosome 11: location of the genes for catalase calcitonin, and insulin-like growth factor II.
Proc. Nat. Acad. Sci. 82: 5064 - 5067, 1985. 16. Lush, I. E. : The Biochemical Genetics of Vertebrates Except Man.
Philadelphia: W. B. Saunders (pub. ) 1966. 17. Mannens, M. ; Slater, R. M. ; Hosting, C. ; Black, J. ; Hoovers, J. ; Bleeder-Wage makers, E. M. ; Vote, P.
A. ; Can, N. ; France, R. R. ; Pearson, P. L. : Chromosome 11, Wilms' tumour and associated congenital diseases. (Abstract) Cytogenet. Cell Genet. 46: 655 only, 1987. 18. Matsubara, S. ; Suter, H. ; Aebi, H. : Fractionation of erythrocyte catalase from normal, hypocatalatic and acatalectic humans. Humangenetik 4: 29 - 41, 1967. 19.
Matsunaga, T. ; Seger, R. ; Home, P. ; Tiefenauer, L. ; Hitzig, W. H. : Congenital acatalasemia: a study of neutrophil functions after provocation with hydrogen peroxide. Predict. Res. 19: 1187 - 1190, 1985. 20. Nance, W. E. ; Empson, J.
E. ; Bennett, T. W. ; Larson, L. : Haptoglobin and catalase loci in man: possible genetic linkage. Science 160: 1230 - 1231, 1968. 21. Narahara, K. ; Niikawa, K. ; Kimira, S. ; Kimono, H. ; Ogata, M. ; Kasai, R. ; Hamawaki, M. ; Matsuoka, K. : Regional mapping of catalase and Wilms tumor-aniridia, genitourinary abnormalities, and mental retardation triad loci to the chromosome segment 11 p 1305 -p 1306. Hum. Genet. 66: 181 - 185, 1984. 22.
Niikawa, N. ; Fukushima, Y. ; Taniguchi, N. ; Iizuka, S. ; Kajii, T. : Chromosome abnormalities involving 11 p 13 and low erythrocyte catalase activity. Hum. Genet. 60: 373 - 375, 1982. 23. Ogata, M. : Acatalasemia. Hum. Genet. 86: 331 - 340, 1991. 24.
Quan, F. ; Korneluk, R. G. ; MacLeod, H. L. ; Tsui, L. C. ; Gravel, R.
A. : An RFLP associated with the human catalase gene. Nucleic Acids Res. 13: 8288 only, 1985. 25. Quan, F. ; Korneluk, R. G. ; Tropak, M. B. ; Gravel, R. A. : Isolation and characterization of the human catalase gene.
Nucleic Acids Res. 14: 5321 - 5335, 1986. 26. Roychoudhury, A. K. ; Nei, M. : Human Polymorphic Genes: World Distribution. New York: Oxford Univ. Press (pub. ) 1988. 27. Schroeder, W.
T. ; Saunders, G. F. : Localization of the human catalase and apolipoprotein A-I genes to chromosome 11. Cytogenet. Cell Genet. 44: 231 - 233, 1987. 28. Shaffer, J. B. ; Preston, K.
E. : Molecular analysis of an acatalasemic mouse mutant. Biochem. Biophys. Res.
Commun. 173: 1043 - 1050, 1990. 29. Shibata, Y. ; Higashi, T. ; Hire, H. ; Hamilton, H. B. : Immuno chemical studies on catalase. II. An anti catalase reacting component in normal hypocatalasic, and acatalasic human erythrocytes. Arch.
Biochem. 118: 200 - 209, 1967. 30. Szeinberg, A. ; De Vries, A. ; Pinkhas, J. ; Djaldetti, M. ; Ezra, R. : A dual hereditary red blood cell defect in one family: hypocatalasemia and glucose- 6 -phosphate dehydrogenase deficiency. Acta Genet. Med. Gemellol. 12: 247 - 255, 1963. 31. Takahara, S. ; Miyamoto, H. : Three cases of progressive oral gangrene due to lack of catalase in the blood.
Nippon Jibi-Inkoka Gakkai Kaiho 51: 163 only, 1948. 32. Wen, J. K. ; Osumi, T. ; Hashimoto, T. ; Ogata, M. : Molecular analysis of human acatalasemia: identification of a splicing mutation. J.
More. Biol. 211: 383 - 393, 1990. 33. Wieacker, P. ; Mueller, C. R. ; Mayerova, A. ; Grzeschik, K.
H. ; Ropers, H. H. : Assignment of the gene coding for human catalase to the short arm of chromosome 11. Ann. Genet. 23: 73 - 77, 1980.
Free research essays on topics related to: hydrogen peroxide, gene, nucleic acids, cat, molecular weight
Research essay sample on Nucleic Acids Hydrogen Peroxide
