Organ culture of adult guinea-pig intestine. II. Biochemical and ultracytochemical findings.
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Alkaline Phosphatase↗
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Results for “THIAMINE PYROPHOSPHATE”
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Histochemical studies on the changing enzyme pattern at the lumen formation in the solid sinus vagina in mouse.
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Age Factors↗
Properties and function of the pyruvate: ferredoxin oxidoreductase from the blue-green alga Anabaena cylindrica.
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Adenosine Triphosphate↗
[Influence of pancreatic juice on phosphorylation and resorption of vitamin B1].
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Adenosine Triphosphate↗
The fine structural localisation of thiamine pyrophosphatase and adenosine triphosphatase in neural tumours induced by N-ethyl-N-nitrosourea in rats.
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Adenosine Triphosphatases↗
Histochemical observations on NDPase and TPPase in cerebral tumours.
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Astrocytoma↗
Accumulation of smooth cisterns, multivesicular bodies and "zebra" bodies in neurons. A case of peculiar storage condition.
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Acid Phosphatase↗
Contribution to the histoenzymology of subacute sclerosing panencephalitis.
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Acetylcholinesterase↗
The role of thiamine in nervous tissue.
The possibility that thiamine (vitamin B1) has a role in nervous tissue that is independent of its well-documented coenzyme function is discussed. After reviewing the localization and metabolism of the vitamin and its phosphate esters, the effects of either thiamine deprivation or antimetabolites of thiamine on conduction and transmission, and the relationship between thiamine triphosphate and the genetic, neurological disease, subacute necrotizing encephalomyelopathy (Leigh's disease), it is suggested that despite the lack of hard evidence, it is likely that the vitamin possesses this alternate function.
Animals↗
Structure and histochemistry of the normal intestine of the fowl. I. The mature absorptive cell.
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Acid Phosphatase↗
Minor salivary glands of man: enzyme and mucosubstance histochemical studies.
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Adenosine Triphosphatases↗
Salivary glands of the cat: a histochemical study.
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Acid Phosphatase↗
Structure and histochemistry of the normal intestine of the fowl. II. Distribution of enzyme activities in the duodenal and jejunal mucosa.
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Adenosine Triphosphatases↗
The formation and continuity of secretion granules in the splenic lobe of the pigeon pancreas as revealed by freeze-etching, micro-x-ray analysis and cytochemistry.
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Adenosine Triphosphatases↗
Photoacoustic spectroscopy and its use in biology. Review.
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Acoustics↗
[Histochemical investigations of the eye of the blowfly Calliphora erythrocephala Meig. II. Nucleosidephosphatases, thiaminepyrophosphatase, nonspecific esterase, and cholinesterase].
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Acetylcholine↗
[Therapy of diabetes mellitus with cocarboxylase; the relations to creatine metabolism].
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Biochemical Phenomena↗
Characterization of the multiple transport routes for methotrexate in L1210 cells using phthalate as a model anion substrate.
o-Phthalate is actively transported into L1210 cells and the primary route for cell entry is the same transport system which mediates the influx of methotrexate and other folate compounds. The identity of the influx route has been established by the following observations: (A) Phthalate influx is competitively inhibited by methotrexate and the inhibition constant (Ki) is comparable to the Kt for half-maximal influx of methotrexate: (B) Various anions inhibit the influx of phthalate and methotrexate with comparable Ki values; (C) The influx of phthalate and methotrexate both fluctuate in parallel with changes in the anionic composition of the external medium; and (D) A specific covalent inhibitor of the methotrexate transport system (NHS-methotrexate) also blocks the transport of phthalate. In contrast, the efflux of phthalate does not occur via the methotrexate influx carrier, but rather by two separate processes which can be distinguished by their sensitivities to bromosulfophthalein. Efflux via the bromosulfophthalein-sensitive route constitutes 75% of total efflux and is enhanced by glucose and inhibited by oligomycin. The inability of phthalate to exit via the methotrexate influx carrier is due to competing intracellular anions which prevent phthalate from interacting with the methotrexate binding site at the inner membrane surface.
Animals↗