1988
DOI: 10.1002/elps.1150090305
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Isoelectric focusing of catalase from acatalasemic mouse and human blood, and cultured human skin fibroblasts

Abstract: 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 i… Show more

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Cited by 14 publications
(3 citation statements)
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“…This catalase is rapidly degraded and has a different electrophoretic mobility [4, 51. The Japanese type of this syndrome indicated no substantial difference between normal and acatalasemic erythrocytes in the charge of catalase protein or molecular size [6,71. A guanine to adenine substitution at the fifth position of intron four (a splice site mutation) seems to be responsible for the defective catalase synthesis in the Japanese type of acatalasemia.…”
mentioning
confidence: 99%
“…This catalase is rapidly degraded and has a different electrophoretic mobility [4, 51. The Japanese type of this syndrome indicated no substantial difference between normal and acatalasemic erythrocytes in the charge of catalase protein or molecular size [6,71. A guanine to adenine substitution at the fifth position of intron four (a splice site mutation) seems to be responsible for the defective catalase synthesis in the Japanese type of acatalasemia.…”
mentioning
confidence: 99%
“…The residual catalase of the Japanese type does not differ from the normal enzyme with respect to isoelectric point, heat stabil ity and molecular weight [4,5]. On the other hand, in Swiss-type acatalasemia the resid ual catalase activity exhibits a higher mobil-We presented a preliminary report on 2 acatalasémie sisters in Hungary [13].…”
Section: Introductionmentioning
confidence: 99%
“…Catalase was detected [4] by immersing the gel plate in 1 % H2C>2 for 5 s, followed by transfer into a vessel containing 50 ml of a 1 % KI solution, adjusted to pH 3.0 with 7% acetic acid. The staining of starch proceeded slowly until all but the area of catalase activity was stained.…”
Section: Isoelectric Focusing Of Catalasementioning
confidence: 99%