Výsledky vyhledávání - "N A, Morjana"

Degradation of human cardiac troponin I after myocardial infarction

Autor: N A, Morjana

Publikováno v: Biotechnology and applied biochemistry. 28(2)

Cardiac troponin I (TnI) is the inhibitory subunit of the troponin complex and a specific biochemical marker for myocardial infarction (MI). It is released into the bloodstream within 4-6 h following MI, peaks after 18-24 h and remains elevated for u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b02b391e9fea672a6d56fa5c33004cb2
https://pubmed.ncbi.nlm.nih.gov/9756462

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Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for a slow conformational change upon coenzyme binding

Autor: T J, Kubiseski, D J, Hyndman, N A, Morjana, T G, Flynn

Publikováno v: The Journal of biological chemistry. 267(10)

Steady state kinetic analysis at pH 7.0 of the reduction of DL-glyceraldehyde by pig muscle aldose reductase showed that the enzyme follows a sequential ordered mechanism with NADPH binding first. However, the "off constant" for NADP+ in the forward

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9572b54a820c481a20667dc9bbeacd93
https://pubmed.ncbi.nlm.nih.gov/1551865

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Correction: Guanidine Hydrochloride Stabilization of a Partially Unfolded Intermediate During the Reversible Denaturation of Protein Disulfide Isomerase

Autor: N. A. Morjana

Publikováno v: Proceedings of the National Academy of Sciences. 90:7908a-7908

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c7e10510a1cb380d51f1cae1d4342242
https://doi.org/10.1073/pnas.90.16.7908a

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Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine

Autor: N A, Morjana, C, Lyons, T G, Flynn

Publikováno v: The Journal of biological chemistry. 264(5)

The reaction of aldose reductase from human psoas muscle with either pyridoxal 5'-phosphate (PLP) or pyridoxal 5'-diphospho-5'-adenosine (PLP-AMP) results in a pseudo first-order 2-fold activation of the enzyme with the stoichiometric incorporation o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9968c8a2c158d74433611fdf83a1d8a7
https://pubmed.ncbi.nlm.nih.gov/2492527

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Studies on the active site of the Neurospora crassa plasma membrane H+-ATPase with periodate-oxidized nucleotides

Autor: A P, Bidwai, N A, Morjana, G A, Scarborough

Publikováno v: The Journal of biological chemistry. 264(20)

The Neurospora crassa plasma membrane H+-ATPase is inactivated by the periodate-oxidized nucleotides, oATP, oADP, and oAMP, with oAMP the most effective. Inhibition of the ATPase is essentially irreversible, because Sephadex G-50 column chromatograph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::356a3cd47182ffedd68114166a89a8c8
https://pubmed.ncbi.nlm.nih.gov/2545685

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Aldose reductase from human psoas muscle. Purification, substrate specificity, immunological characterization, and effect of drugs and inhibitors

Autor: N A, Morjana, T G, Flynn

Publikováno v: The Journal of biological chemistry. 264(5)

Aldose reductase (ALR2) has been purified to homogeneity from human psoas muscle. From sodium dodecyl sulfate-polyacrylamide electrophoresis the enzyme is monomeric and has a molecular weight of 37,000. ALR2 catalyzes the primarily NADPH-dependent re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ee90f9d7389445d154b811a9b75f0e4c
https://pubmed.ncbi.nlm.nih.gov/2492526

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