Acatalasemic Mice

Feinstein, Robert N.; Seaholm, John E.; Howard, Judith B.; Russell, William D.

doi:10.1073/pnas.52.3.661

Cited by 35 publications

(12 citation statements)

References 5 publications

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“…In order to have an analogous condition suitable for experimental studies, extensive screenings for hypocatalasemic mice were performed by Feinstein et al (1964). Five mice, mutant with respect to blood catalase, were obtained.…”

Section: Introductionmentioning

confidence: 99%

Activity and stability of catalase in blood and tissues of normal and acatalasemic mice

1968

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Catalase activity in blood, liver, and kidney of a mutant strain Cs b has been found to be decreased as compared to the level in normal mice. However, the extent of the reduction largely depends on the conditions used for activity determination, in particular, temperature and duration of the incubation period. In liver, this effect is most pronounced, the observed activity in mutants varying between 21 and 85% of the normal level This dependence on the assay conditions is mainly due to the unusual heat lability of the variant enzyme, which undergoes rapid inactivation when incubated at 37 C.

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Section: Introductionmentioning

confidence: 99%

Activity and stability of catalase in blood and tissues of normal and acatalasemic mice

1968

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“…This mutation resembles those thoroughly investigated by Feinstein et al [11,12] Purified normal erythrocyte catalase, when kept in dilute solution, or hemolysates, when highly diluted, soon loose catalase activity. On the other hand, they are rather stable when kept concentrated [7,20], This probably explains the lower yield observed when preparing the acatalasémie catalase preparation.…”

Section: Discussionmentioning

confidence: 96%

Nature of Residual Erythrocyte Catalase Activity in Swiss-Type Acatalasemia

Shapira¹,

Ben‐Yoseph²,

Aebi³

1974

Enzyme

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It has been shown by means of a specific anticatalase antibody preparation that there is only partial immunological identity between catalase obtained from normal red cells and the variant enzyme from an individual homozygous for Swiss-type acatalasemia. Further data, such as descreased stability against heat and concentrated urea, support the assumption that the low level of catalase activity (~2% of normal) found in hemolysates is due to an instability of the mutant enzyme.

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“…Feinstein has demonstrated the feasibility of such an approach by recovering catalase variants from X-irradiated stocks. 56 Such markers in the mouse would constitute valuable material for somatic cell genetic studies.…”

Section: Drug Resistance Mutantsmentioning

confidence: 99%

Linkage Analysis Using Somatic Cell Hybrids

Ruddle

1972

Advances in Human Genetics

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Acatalasemic Mice

Cited by 35 publications

References 5 publications

Activity and stability of catalase in blood and tissues of normal and acatalasemic mice

Activity and stability of catalase in blood and tissues of normal and acatalasemic mice

Nature of Residual Erythrocyte Catalase Activity in Swiss-Type Acatalasemia

Linkage Analysis Using Somatic Cell Hybrids

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