Histochemical and cytochemical demonstration of Ca++-ATPase activity in the stellate cells of the adenohypophysis of the guinea pig

1985 ◽  
Vol 83 (3-4) ◽  
pp. 195-200 ◽  
Author(s):  
H. J. Bambauer ◽  
S. Ueno ◽  
H. Umar ◽  
M. Ueck
Keyword(s):  
Guinea Pig ◽  
Atpase Activity ◽  
Stellate Cells ◽  
Cytochemical Demonstration

scholarly journals Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical myosin ATPase and anti-myosin monoclonal antibodies.

1990 ◽  
Vol 38 (2) ◽  
pp. 257-265 ◽  
Author(s):  
L Gorza
Keyword(s):  
Monoclonal Antibodies ◽  
Guinea Pig ◽  
Atpase Activity ◽  
High Activity ◽  
Skeletal Muscles ◽  
Enzyme Histochemistry ◽  
Myosin Atpase ◽  
Myosin Atpase Activity ◽  
Combined Use

A novel type of myosin heavy chain (MHC), called 2X, has been recently identified in type 2 fibers of rat skeletal muscles using an immunochemical approach. In the present study, the same panel of anti-MHC monoclonal antibodies was used in immunohistochemistry combined with enzyme histochemistry to identify and compare type 2X fibers in hindlimb skeletal muscles of rat, mouse, and guinea pig. Immunohistochemistry shows that 2X MHC is localized in a large subset of type 2 fibers and is co-expressed with 2A or 2B MHC in a small number of fibers. Enzyme histochemistry shows that type 2X fibers display low myosin ATPase activity after pre-incubation at pH 4.3 and high activity after paraformaldehyde pre-incubation at pH 10.4. After pre-incubation at pH 4.6, myosin ATPase shows intermediate and high activity in rat and mouse 2X fibers, respectively, whereas it is low in guinea pig 2X fibers. Succinate dehydrogenase displays moderate to high activity in 2X fibers of all species. Taken together, these staining patterns allow this novel fiber population to be distinguished from the other type 2 fibers using only enzyme histochemistry. Nevertheless, the combined use of immuno- and enzyme histochemistry prevents incorrect fiber typing due to the interspecies variability of myosin ATPase activity among the correspondent fiber types, and completely modifies the presently used classification of mouse type 2 fibers.

scholarly journals Effects of divalent cations and La3+ on contractility and ecto-ATPase activity in the guinea-pig urinary bladder

1995 ◽  
Vol 114 (3) ◽  
pp. 632-639 ◽  
Author(s):  
Airat U. Ziganshin ◽  
Lilia E. Ziganshina ◽  
Charles H.V. Hoyle ◽  
Geoffrey Burnstock
Keyword(s):  
Urinary Bladder ◽  
Guinea Pig ◽  
Atpase Activity ◽  
Divalent Cations

Digitalis-like biological activity in rat cerebellum

1986 ◽  
Vol 64 (10) ◽  
pp. 1049-1053 ◽  
Author(s):  
Steven P. Lintlop ◽  
Bill Durante ◽  
Fred A. Sunahara ◽  
Amar K. Sen
Keyword(s):  
Biological Activity ◽  
Guinea Pig ◽  
Atpase Activity ◽  
Rat Brain ◽  
Inhibitory Activity ◽  
Regulatory Mechanism ◽  
Ouabain Binding ◽  
Rat Brain Synaptosomes ◽  
Rat Cerebellum ◽  
Brain Synaptosomes

The cytosolic fraction of rat cerebellum possesses a factor(s) which is capable of inhibiting synaptosomal Na,K-ATPase activity, competing with [3H]ouabain binding to rat brain synaptosomes, and inducing positive inotropy in guinea pig atrial strips. These results demonstrate the existence of a ouabain-like principle in rat cerebella. The inhibitory activity of the factor was found to be partially thermolabile and diminished by a proteolytic agent, and the activity could be augmented by increasing concentrations of Mg2+, suggesting a regulatory mechanism for the endogenous digitalis-like principle.

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