Ultrastructural localization of alpha-OH acid oxidase in peroxisomes with the CeCl3 technique. | Zendy

Gail Ferstandig Arnold | Zendy; E Holtzman | Zendy

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Ultrastructural localization of alpha-OH acid oxidase in peroxisomes with the CeCl3 technique.

Author(s) -

Gail Ferstandig Arnold,

E Holtzman

Publication year - 1980

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/28.9.6997367

Subject(s) - peroxisome , substrate (aquarium) , microbody , biochemistry , alpha (finance) , chemistry , butyrate , oxidase test , glutaraldehyde , enzyme , biology , chromatography , medicine , ecology , construct validity , nursing , fermentation , patient satisfaction , gene

alpha-OH acid oxidase activity was demonstrated in peroxisomes of glutaraldehyde-fixed tissues using the CeCl3 cytochemical method. For kidney, alpha-OH butyrate or alpha-OH valerate were used as substrates. These substrates gave much less reaction product in liver peroxisomes. Liver peroxisomes were more reactive with glycolate as substrate. Glycolate gave little or no reaction product in kidney peroxisomes. alpha-keto-glutarate inhibited activity of the enzyme with alpha-OH butyrate as substrate.

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