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FURTHER INVESTIGATION OF HISTOCHEMISTRY OF FRUCTOSE‐1,6‐DIPHOSPHATE d ‐GLYCERALDEHYDE‐3‐PHOSPHATE‐LYASE IN THE RAT BRAIN
Author(s) -
Maeda T.,
Shimizu N.,
Wegmann R.
Publication year - 1968
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1968.tb08949.x
Subject(s) - chemistry , glyceraldehyde , biochemistry , aldolase a , enzyme , white matter , fructose , staining , dehydrogenase , biology , medicine , magnetic resonance imaging , radiology , genetics
— The distribution of fructose‐1,6‐diphosphate d ‐glyceraldehyde‐3‐phosphate‐lyase (I.U.B. 4.1.2.13) (fructose diphosphate aldolase) in brain sections fixed by alcohol was studied using a gelled substrate mixture containing d ‐glyceraldehyde‐3‐phosphate: NAD oxidoreductase (I.U.B. 1.2.1.12) and phenazine methosulphate. The formazan precipitation pattern in brain sections depends on the experimental conditions determining the affinity of the complex of Nitro‐blue tetrazolium and phenazine methosulphate to tissue components. The complex is unable to precipitate on the white matter in fresh sections but alcohol fixation increases its affinity to the white matter and decreases it to the neuropil. Using the modified histochemical method, aldolase activity in the brain was seen both in the gray and white matter. Although the distribution of this enzyme activity in the gray matter was generally identical with that obtained previously, in the present study enzyme activity was found in the paraventricular structures and in the white matter where negative activity was previously obtained.