FINE STRUCTURAL LOCALIZATION OF ADENINE NUCLEOSIDE PHOSPHATASE ACTIVITY IN THE SARCOPLASMIC RETICULUM OF STRIATED MUSCLE11This work was supported by a grant from the Danish State Research Foundation.,22The following abbreviations are used in this chapter: AMP, ADP, ATP: adenosine-monophosphate, adenosine diphosphate, adenosine triphosphate; AMPase, ADPase, ATPase: adenosinemonophosphatase, adenosinediphosphatase, adenosinetriphosphatase; TPP: thiamine pyrophosphate.

1966 ◽  
pp. 103-118
Author(s):  
J. ROSTGAARD ◽  
O. BEHNKE
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Phosphatase Activity ◽  
Adenosine Triphosphate ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Thiamine Pyrophosphate ◽  
Structural Localization ◽  
State Research

scholarly journals AN ELECTRON MICROSCOPY STUDY OF PHOSPHATASE ACTIVITY IN THE ENDOTHELIAL CELLS OF RABBIT AORTA

1966 ◽  
Vol 14 (10) ◽  
pp. 719-724 ◽  
Author(s):  
HENRY F. HOFF ◽  
JÜRG GRAF
Keyword(s):  
Phosphatase Activity ◽  
Rabbit Aorta ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Microscopy Study ◽  
Electron Microscopy Study ◽  
Endothelial Lining ◽  
Structural Localization ◽  
Pinocytotic Vesicles

The fine structural localization of phosphatase activity in the endothelial lining of rabbit aorta was studied using the electron microscope. The tissue was incubated in media containing various substrates at different pH values. Only a neutral phosphatase activity was localized with a preferential specificity for adenosine triphosphate (ATP), although some affinity was found with adenosine diphosphate, adenosine monophosphate, β-glycerophosphate and phenylphosphate. The reaction product (lead phosphate), with ATP and ADP as substrates, was localized primarily in cell membrane invaginations at the intercellular spaces and in neighboring pinocytotic vesicles, and only slightly in similar invaginations at the luminal and intimal surfaces. Enzyme localization was similar using the other substrates, but with a lower concentration of reaction product that was absent from the invaginations at the luminal surface. The significance of these observations in light of the role of cytopempsis in intimal nutrition and pathogenesis of atherosclerosis is briefly discussed.

Selective sensing of adenosine monophosphate (AMP) over adenosine diphosphate (ADP), adenosine triphosphate (ATP), and inorganic phosphates with zinc(II)-dipicolylamine-containing gold nanoparticles

2021 ◽  
Author(s):  
Lena Reinke ◽  
Marcus Koch ◽  
Christine Müller-Renno ◽  
Stefan Kubik
Keyword(s):  
Gold Nanoparticles ◽  
Adenosine Triphosphate ◽  
Triethylene Glycol ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Mixed Monolayer ◽  
Inorganic Phosphates

Mixed monolayer-protected gold nanoparticles containing surface-bound triethylene glycol and dipicolylamine groups aggregated in water/methanol, 1:2 (v/v) in the presence of nucleotides, if the solution also contained zinc(II) nitrate to convert...

scholarly journals ON THE LOCALIZATION OF SOME PHOSPHATASES IN THREE DIFFERENT SEGMENTS OF THE PROXIMAL TUBULES IN THE RAT KIDNEY

1967 ◽  
Vol 15 (8) ◽  
pp. 456-469 ◽  
Author(s):  
N. O. JACOBSEN ◽  
F. JØRGENSEN ◽  
Å. C. THOMSEN
Keyword(s):  
Adenosine Triphosphate ◽  
Rat Kidney ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Proximal Tubules ◽  
Reaction Pattern ◽  
Cytoplasmic Bodies ◽  
Acid And Alkaline Phosphatase ◽  
Convoluted Tubules

The distribution of several phosphatases in three segments of the proximal tubules was studied in frozen sections of glutaraldehyde-fixed rat kidneys. Two segments of the convoluted tubules were identified by in vivo injection of trypan blue. By increasing the concentration of adenosine triphosphate to 3 mM in the Wachstein and Meisel ATPase medium, a clear segmental differentiation in the reaction pattern of the brush border, cytoplasmic bodies and basal infoldings of the proximal tubules was obtained. The specificity of the reaction was investigated by substituting adenosine diphosphate, adenosine monophosphate or β-glycerophosphate for adenosine triphosphate in the incubation medium and by employing cyanide or fluoride as inhibitors. The reaction pattern was also compared with the localization of acid and alkaline phosphatase activities. In addition, the distribution of glucose 6-phosphatase activity was studied which showed differences in the three segments of the proximal tubules.

FACTORS INFLUENCING TETRAZOLE REDUCTION BY REDUCED NICOTINAMIDE–ADENINE DINUCLEOTIDE IN PIGEON-HEART MITOCHONDRIA

1967 ◽  
Vol 45 (2) ◽  
pp. 299-307 ◽  
Author(s):  
C. L. Talesara ◽  
M. C. Blanchaer
Keyword(s):  
Adenosine Triphosphate ◽  
Respiratory Chain ◽  
Nicotinamide Adenine Dinucleotide ◽  
Inorganic Phosphate ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Heart Mitochondria ◽  
Nicotinamide Adenine ◽  
Tetrazolium Chloride ◽  
Reduced Nicotinamide Adenine Dinucleotide

The effect of adenosine triphosphate, adenosine diphosphate, adenosine monophosphate and inorganic phosphate on the reduction of 2-(p-iodophenyi)-3-p-nitrophenyl-5-phenyl tetrazolium chloride (INT) to its formazan by reduced nicotinamide-adenine dinucleotide (NADH) was studied in pigeon-heart mitochondria. Formazan production was followed at 540 mμ in 2.2 ml medium containing 0.4–0.5 mg mitochondrial protein, 0.22 M mannitol, 0.067 M sucrose, 0.02 M Tris–chloride, 0.02 mM EDTA, 0.5–3.0 mM INT, and 38 μM NADH at pH 7.2 and 28 °C. By means of the respiratory inhibitors Amytal, rotenone, antimycin A, and cyanide, it was shown that INT diverts electrons from the respiratory chain principally at the flavoprotein level. In contrast to its inhibitory effect on "the O2-linked oxidation of NADH, 10 mM adenosine triphosphate stimulated the reaction rate and formazan yield in the present system. Equimolar inorganic phosphate also increased the initial velocity but adenosine diphosphate and adenosine monophosphate did not. Preliminary kinetic studies suggest that NADH, but not INT, combines with the form of NADH dehydrogenase in the respiratory chain with which adenosine triphosphate reacts.

The Effect of the Alkyl Tins on Platelet Aggregation

1963 ◽  
Vol 09 (02) ◽  
pp. 330-334 ◽  
Author(s):  
Dr. J. R O’Brien
Keyword(s):  
Platelet Aggregation ◽  
Adenosine Triphosphate ◽  
Platelet Rich Plasma ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate

SummaryThe addition of the tri alkyl tins to stirred platelet rich plasma produces after a delay, gross platelet aggregation. The delay is decreased by Adenosine triphosphate and increased by Adenosine monophosphate. The tri alkyl tins may liberate Adenosine diphosphate from the platelets, possibly by stimulating an ATP-ase. Plasma as well as platelets can inactivate Adenosine diphosphate.

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