Catalase Activity of Immature and Mature Red Cells from Acatalasemic Mouse Mutant

Ogata, Masana; Inoue, Takato; Tomokuni, K; Takahara, Shigeo

doi:10.1159/000208657

Cited by 11 publications

(4 citation statements)

References 12 publications

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“…Catalase activity depends on the assay temperature due to the heat instability of the variant enzyme (Tottori 1987). The catalase activity in acatalasemic mice is low in reticulocytes, yet its degradation by maturation is considerably great (Ogata et al 1970). In acatalasemic mice, catalase subunits expressing peroxidative activity are present in the liver (Srivastava and Ansari 1980).…”

Section: Catalase Activitymentioning

confidence: 99%

“…Normal activity (%) Cellular distribution in blood (ratio of activity in reticulocytes to activity in erythrocytes Activity in tissues relative to normal Catalase activity in heterozygotes (hypocatalasemia) Japanese 0.16 _+ 0.02 Slightly higher but not (Ogata et al 1972) significantly different 0.39 _+ 0.23 from normal (1.4-5.6) (Takahara et al 1977) (Ogata et al 1972) Swiss 1.08 + 0.34 Much higher (300-400) (Aebi et al 1964) (Aebi et al 1966) Mutant mice 4.40 +_ 0.30 (Tottori 1987) Moderately higher (25) (Ogata et al 1970) Trace in vermiform appendix (2.7%) Abdominal muscle (UDS) a Cultured skin fibroblasts (2.2%) (Sadamoto 1966) Liver (< 0.01%), placenta (15%), tonsilla (3%) (Aebi et al 1964) Cultured skin fibroblasts (15%) (Krooth et al 1962) Liver (65.7%), kidneys (15.6%), lungs (69.9%) (Tottori 1987) Cultured transformed fibroblast Cell line (30%) (Lewis 1985) Half normal (Takahara et al 1960) Within normal range (Aebi et al 1977) Half normal (Feinstein et al 1966) a UDS, Under detectable sensitivity (Ogata 1989(Ogata ) 1972(Ogata , 1989) (blood, fibroblasts)…”

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confidence: 99%

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Acatalasemia

Ogata

1991

Hum Genet

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The abnormalities in acatalasemia at the gene level as well as properties of the residual catalase in Japanese acatalasemia are historically reviewed. The replacement of the fifth nucleic acid, guanine, in the fourth intron by adenine in the acatalasemic gene causes a splicing mutation and hence a deficiency of mRNA. The guanine-to-adenine substitution was detected in two Japanese acatalasemic cases from different families. The properties of the residual catalase are similar to those of normal catalase; the exons are identical. The properties of the residual catalase and the molecular defect in the catalase gene are compared among Japanese, Swiss, and mouse acatalasemias. The physiological role of catalase, as judged from human acatalasemic blood and acatalasemic mice, is also described.

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Section: Catalase Activitymentioning

confidence: 99%

mentioning

confidence: 99%

Acatalasemia

Ogata

1991

Hum Genet

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“…In the mutant mice, the residual catalase activity is present mainly in reticulocytes, and it decreases with cell maturation, as in Swiss type. It is also heat labile (17). Properties of the erythrocyte catalase in the Japanese type acatalasemia and hypocatalasemia significantly differed from those of the Swiss type and those of the mutant mice.…”

Section: Frequency Of Acatalasemiamentioning

confidence: 93%

“…10). Observations have shown that high catalase activity is lost on the maturation of reticulocytes (17). The liver cell catalase protein of acatalasemic mice was 78 % of the normal level, whereas the specific activity of catalase from the same samples was 31 % of the normal level (22).…”

Section: Frequency Of Acatalasemiamentioning

confidence: 99%

Residual Catalase in Japanese Type Acatalasemia

Ogata

Mizugaki

1978

Cell Struct. Funct.

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Isoelectric focusing of catalase from acatalasemic mouse and human blood, and cultured human skin fibroblasts

Ogata

Satoh

1988

Electrophoresis

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Hemolysates of normal, heterozygous hypocatalasemic and acatalasemic mice and of Japanese acatalasemic subjects were separated into three fractions, A, B and C, by DEAE-cellulose column chromatography, and pI values of A, B and C fractions were determined by isoelectric focusing. The pI value of catalase in the A, B and C fractions increased in the order of normal, hypocatalasemic and acatalasemic mouse blood. The results obtained from Japanese acatalasemic blood samples showed that the pI values of catalase in the A, B and C fractions were similar to those in normal blood. Catalase in Japanese acatalasemic cultured skin fibroblasts was also analyzed by isoelectric focusing. The pI values of catalase in the extract from the cultured skin acatalasemic fibroblasts was similar to that in normal fibroblasts.

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Catalase Activity of Immature and Mature Red Cells from Acatalasemic Mouse Mutant

Cited by 11 publications

References 12 publications

Acatalasemia

Acatalasemia

Residual Catalase in Japanese Type Acatalasemia

Isoelectric focusing of catalase from acatalasemic mouse and human blood, and cultured human skin fibroblasts

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