The histochemical demonstration of myofibrillar adenosine triphosphatase activity in fish muscle

1974 ◽  
Vol 52 (7) ◽  
pp. 871-877 ◽  
Author(s):  
I. A. Johnston ◽  
S. Patterson ◽  
P. Ward ◽  
G. Goldspink

A technique for the demonstration of myofibrillar adenosine triphosphatase activity (ATPase) used for mammalian muscle has been modified to suit fish muscle. The mammalian method involves selectively inhibiting fiber types by preincubation at either alkaline (pH 10.4) or acid (pH 4.3) pH before incubation for myofibrillar (ATPase) activity. Fish muscle fibers were found to be generally inactivated under these conditions. Preincubation at an acid pH was found to be unsuitable for fish muscle because of the indiscriminate inactivation of the fibers. The effects of preincubating at pH 10.4 and incubating tissue sections for different time periods and at different pH's and temperatures have been investigated. A differential staining of fiber types correlated with biochemical data on myofibrillar ATPase for red and white muscles was obtained by preincubating sections for short periods (1–2 min) at pH 10.4. Under these conditions the intermediately positioned pink fibers were found to stain similarly to the white fibers of high myofibrillar ATPase activity. An investigation has been made of the qualitative distribution of fiber types in the myotomal muscle of live teleost species: coalfish (Gadus virens), grey mullet (Mugil cephalus), crucian carp (Carassius carassius), black mollie (Mollienesia sp), and glassfish (Chanda ranga). The pink fibers were found to be abundant in all the species examined with the exception of the glassfish.

1962 ◽  
Vol 202 (5) ◽  
pp. 940-946 ◽  
Author(s):  
Norman R. Alpert ◽  
Michael S. Gordon

Myofibrillar adenosine triphosphatase (ATPase) activity from seven failing and nine control hearts was studied. The failing hearts came from patients with a clinical and pathological diagnosis of congestive heart failure following benign essential hypertension. Normal hearts were obtained following traumatic death in otherwise normal subjects with no evidence of pathology. As the MgCl2 concentration was increased, the myofibrillar ATPase from the failing hearts exhibited a significantly lower rise in activity than that from the normal hearts. Increasing the substrate concentration to 5 mm adenosine triphosphate (ATP) increased the myofibrillar ATPase activity to an optimum of .95 µm/mg/15 min in the normal group and .69/µm/ mg/15 min in the failing group. Further increases in substrate concentration decreased the ATPase activity in both groups. It was concluded that myofibrils from a heart in congestive failure following benign essential hypertension hydrolyze ATP at a slower rate than those from normal hearts. Since myofibrillar ATPase activity and tension development go hand in hand, the decrease in ATPase activity in the failing heart may account for its inability to meet the work load imposed upon it. Thus these experiments offer evidence that a lesion in congestive heart failure may reside in the contractile protein itself.


1977 ◽  
Vol 162 (3) ◽  
pp. 665-670 ◽  
Author(s):  
F Gibson ◽  
G B Cox ◽  
J A Downie ◽  
J Radik

A plasmid was isolated which included the region of the Escherichia coli chromosome carrying the known genes concerned with oxidative phosphorylation (unc genes). This plasmid was used to prepare partial diploids carrying normal unc alleles on the episome and one of the three mutant alleles (unc A401, uncB402 or unc-405) on the chromosome. These strains were compared with segregants from which the plasmid had been lost. Dominance of either normal ormutant unc alleles was determined by growth on succinate, growth yields on glucose, Mg-ATPase (Mg2+-stimulated adenosine triphosphatase) activity, atebrin-fluorescence quenching, ATP-dependent transhydrogenase activity and oxidative phosphorylation. In all the above tests, dominance of the normal allele was observed. However, in membranes from the diploid strains which carried a normal allele and either of the mutant alleles affecting Mg-ATPase activity (uncA401 or unc-405), the energy-linked functions were only partially restored.


1987 ◽  
Vol 17 (3) ◽  
pp. 479
Author(s):  
Wang Seong Ryu ◽  
Un Ho Ryoo ◽  
Jung Don Seo ◽  
Young Woo Lee

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