A Biochemical Approach for the Study of Uveitis by Protein and LDH-Isoenzyme Analysis of Serum and Aqueous Humor

Papadopoulos, Nicholas M.; Thomas, Edward

doi:10.3181/00379727-131-33899

Experimental Biology and Medicine

1969

DOI: 10.3181/00379727-131-33899

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A Biochemical Approach for the Study of Uveitis by Protein and LDH-Isoenzyme Analysis of Serum and Aqueous Humor

Nicholas M. Papadopoulos

Edward Thomas

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1974

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Cited by 4 publications

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“…The LDH content of normal and cata ractous lenses was also ascertained by Hockwin and Berghoff (8) and corroborated by others (9-11). Papadopolous and Thomas (13) noted the presence of the isoenzymes, LDH3, LDH4 and LDH5 in the clear lens of a cadaver and a similar pattern was reported by Kasavina et al (9) . The occurrence of a number of enzymes in the human lens has been investigated by Friedburg (6) and such work is reviewed and sum marized by him in a recent article.…”

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confidence: 55%

Distribution of Glycolytic Enzymes in Nuclear and Peripheral Lens Sections of the Human Senile Cataract

Ll¹,

Tc²,

Mirza³

1977

Enzyme

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Human nuclear cataracts soon after surgery, were dissected and the nuclear and clearer peripheral portions individually homogenized with physiological saline and centrifuged. The filtrates were analyzed for aldolase, phosphohexose isomerase and lactic dehydrogenase and the 3 enzymes found to range 6—14 times higher in the peripheral than in the nuclear portions of the lens. The LDH isozyme patterns of the peripheral tissue homogenates indicated greater glycolytic activity.

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supporting

confidence: 55%

Distribution of Glycolytic Enzymes in Nuclear and Peripheral Lens Sections of the Human Senile Cataract

Ll¹,

Tc²,

Mirza³

1977

Enzyme

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The thin-layer isoelectric focusing of lactate dehydrogenase isoenzymes in rabbit lens parts and in intraocular tissues

Bours

Neuhaus

Hockwin

1977

Albrecht von Graefes Arch. Klin. Ophthalmol.

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Lactate dehydrogenase (LDH) isoenzymes of rabbit lens and other intraocular tissues are separated by thin-layer isoelectric focusing and localized as discrete groups of multiple bands with defined isoelectric points after staining by the tetrazolium method. In the rabbit lens parts, the predominant isoenzymes are LDH-4 and LDH-5. The bands show microheterogeneity, are composed of 2-4 subcomponents, and the pattern shows a distribution of the liver type. The activity of the LDH-4 decreases and that of LDH-5 increases in an order given by the equator, anterior and posterior cortex, and nucleus. LDH-3 remains almost constant in all lens parts. LDH-4 is composed of two subcomponents, one of which, the most cathodic with higher isoelectric point, is almost absent in the lens nucleus. Of the LDH localized in the rabbit intraocular tissues, only the retina shows a pattern of five isoenzymes also of the liver type. In all intraocular tissues LDH-3, -4, and -5 are very prominent, show also microheterogeneity of their isoenzyme bands, and are each composed of 4-6 subcomponents. LDH-1 and -2 show only one isofocused component. Species specificity is shown of the LDH isoenzymes in the rabbit, mouse, dog, and calf lens.

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Isoenzyme der Lactatdehydrogenase im Glaskörper des Rindes

Hoffmann

Wurster

1974

Albrecht von Graefes Arch. Klin. Ophthalmol.

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A Biochemical Approach for the Study of Uveitis by Protein and LDH-Isoenzyme Analysis of Serum and Aqueous Humor

Cited by 4 publications

References 0 publications

Distribution of Glycolytic Enzymes in Nuclear and Peripheral Lens Sections of the Human Senile Cataract

Distribution of Glycolytic Enzymes in Nuclear and Peripheral Lens Sections of the Human Senile Cataract

The thin-layer isoelectric focusing of lactate dehydrogenase isoenzymes in rabbit lens parts and in intraocular tissues

Isoenzyme der Lactatdehydrogenase im Glaskörper des Rindes

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