PURIFICATION OF GLUTARALDEHYDE ITS SIGNIFICANCE FOR PRESERVATION OF ACID PHOSPHATASE ACTIVITY | Zendy

H. Dariush Fahimi | Zendy; P Drochmans | Zendy; A Popowski | Zendy

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PURIFICATION OF GLUTARALDEHYDE ITS SIGNIFICANCE FOR PRESERVATION OF ACID PHOSPHATASE ACTIVITY

Author(s) -

H. Dariush Fahimi,

P Drochmans,

A Popowski

Publication year - 1968

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 - 10.1177/16.3.199

Subject(s) - glutaraldehyde , acid phosphatase , chemistry , fixation (population genetics) , distilled water , phosphatase , enzyme , biochemistry , enzyme assay , chromatography , gene

The inhibition of acid phosphatase activity in rat liver homogenates after fixation in different lots of commercial glutaraldehyde is determined and compared with the inhibition following fixation with a distilled product. It is shown that commercial glutaraldehydes inhibit more of the enzyme activity than the distilled product. The acidic products of oxidation of glutaraldehyde do not increase the inhibition of the enzymatic activity. The presence of high concentration of inorganic phosphates in different lots of commercial glutaraldehyde, as presented here, suggests that probably such impurities may be responsible for increased inhibition of phosphatase activity noted after fixation in commercial glutaraldehydes.

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