Histochemical Localization of Oxidase Activity in the Mitochondria of the Heart in Some Lower Vertebrates

Nature ◽  
1960 ◽  
Vol 185 (4716) ◽  
pp. 866-867 ◽  
Author(s):  
A. STOLK
Author(s):  
W. Allen Shannon ◽  
Hannah L. Wasserkrug ◽  
andArnold M. Seligman

The synthesis of a new substrate, p-N,N-dimethylamino-β-phenethylamine (DAPA)3 (Fig. 1) (1,2), and the testing of it as a possible substrate for tissue amine oxidase activity have resulted in the ultracytochemical localization of enzyme oxidase activity referred to as DAPA oxidase (DAPAO). DAPA was designed with the goal of providing an amine that would yield on oxidation a stronger reducing aldehyde than does tryptamine in the histochemical demonstration of monoamine oxidase (MAO) with tetrazolium salts.Ultracytochemical preparations of guinea pig heart, liver and kidney and rat heart and liver were studied. Guinea pig kidney, known to exhibit high levels of MAO, appeared the most reactive of the tissues studied. DAPAO reaction product appears primarily in mitochondrial outer compartments and cristae (Figs. 2-4). Reaction product is also localized in endoplasmic reticulum, cytoplasmic vacuoles and nuclear envelopes (Figs. 2 and 3) and in the sarcoplasmic reticulum of heart.


1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.


2008 ◽  
Vol 46 (01) ◽  
Author(s):  
U Merle ◽  
C Eisenbach ◽  
KH Weiss ◽  
S Tuma ◽  
W Stremmel

1960 ◽  
Vol XXXIII (II) ◽  
pp. 255-260 ◽  
Author(s):  
L. S. Ramaswami ◽  
A. B. Lakshman

ABSTRACT By using enzymes, the gonadotrophic factors in the skipper-frog pituitary glands have been selectively inactivated or destroyed. By incubating a known number of pituitary gland homogenate with ptyalin in a constant temperature bath for 5–6 h the follicle-stimulating factor is inactivated; with trypsin or pepsin, the luteinizing factor is inactivated. Bioassay on gravid skipper-frogs indicate that the ptyalin digested homogenate brings about profuse spawning while the trypsin or pepsin digested homogenates do not. When a combination of ptyalin digested and trypsin digested homogenates is injected into fresh gravid skipper-frogs, poor spawning is brought about. These experiments show that the luteinizing factor alone brings about more profuse spawning than when it is combined with the follicle-stimulating factor. It is likely, therefore, that in the lower vertebrates the luteinizing factor of the pituitary gland plays a more predominant role. The exact proportions in which the different dosages for the control and test animals are administered are also tabulated.


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