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Inhibition of CAT enzyme activity in Arabidopsis thaliana (1996)

Röver, Markus ; Matzk, Anja ; Baker, Barbara ; [et al.]

Springer

Plant cell, tissue and organ culture 45 (1996), S. 31-36

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ISSN: 1573-5044

Keywords: chloramphenicol acetyltransferase ; transgenic Arabidopsis thaliana ; transgenic Nicotiana tabacum ; ELISA

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Previously it was shown that transient chloramphenicol acetyltransferase (CAT) marker gene expression in Arabidopsis thaliana and Nicotiana tabacum resulted in significant differences in the accumulation of the CAT reaction products in radioactive CAT assays. Compared to Nicotiana tabacum, conversion of chloramphenicol to the acetylated products in Arabidopsis thaliana extracts was rather low. Here we report that the low CAT enzyme activity can be attributed in part to a heat sensitive CAT inhibitory effect in extracts of Arabidopsis thaliana. CAT enzyme activity in transgenic tobacco is inhibited by extracts from Arabidopsis. This inhibitory effect diminishes when Arabidopsis extracts were heat incubated. CAT activity in transgenic Arabidopsis lines was very low and was only detected in heat incubated extracts. Alternatively, enzyme-linked immunosorbent assays (ELISAs) can be used to detect the CAT protein in transgenic Arabidopsis.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00043425

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An electron microscopic and enzymic study of rat liver peroxisomal nucleoid core and its association with urate oxidase (1977)

Lata, Gene F. ; Mamrak, Frank ; Bloch, Phillip ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Supramolecular Structure 7 (1977), S. 419-434

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ISSN: 0091-7419

Keywords: peroxisome ; microbody ; nucleoid core ; urate oxidase ; starvation effects ; rat liver enzymes ; catalase ; cell organelle ; Life Sciences ; Molecular Cell Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: The appearance of the characteristic crystalloid core of rat liver peroxisomes is emulated by the electron microscopic (EM) appearance of highly purified urate oxidase prepared from the same tissue. The purity of the enzyme preparation was established by gel electrophoresis under various conditions and the specific enzyme activity was at least as high as any previously reported. The amino acid composition of urate oxidase was determined. As additional evidence for close association of the peroxisomal core with urate oxidase, it was demonstrated that the biphasic changes in rat liver urate oxidase activity in response to prolonged starvation were paralleled by changes in the EM appearance of peroxisomes. Under comparable conditions catalase, another peroxisomal enzyme, did not show the same changes in activity as did urate oxidase. Evidence for the possible identity of urate oxidase with the peroxisomal crystalloid of rat liver has been presented, all materials having been obtained from, and experiments performed with, the rat.

Additional Material: 7 Ill.