Dehydrogenase Isoenzymes

Barnett, H.

doi:10.1016/s0140-6736(62)90085-5

Cited by 24 publications

(5 citation statements)

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“…Total serum lactate dehydrogenase activity was determined by the spectrophotometric method of Hill and Levi (1954). The five isoenzymes were estimated by the method already described (Hawkins and Whyley, 1965), using strips stained by Barnett's (1962) method for location, and measuring the individual isoenzyme fractions spectrophotometrically.…”

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confidence: 99%

Quantitative Determinations of Serum Lactate Dehydrogenase Isoenzymes in Cases of Antepartum Haemorrhage

Hawkins

Whyley

1966

BJOG

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confidence: 99%

Quantitative Determinations of Serum Lactate Dehydrogenase Isoenzymes in Cases of Antepartum Haemorrhage

Hawkins

Whyley

1966

BJOG

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“…Preparation of tissue and experiinental animals were the same as described in a previous paper (VAN DEN HENDE et al, 1968). Electrophoresis of the homogenised tissues was performed on cellogel (Chemetron-Milano) in barbiturate buffer p H 8.6, ionic strength 0.05, and was demonstrated by a staining technique described by BARNETT (1962). The relative heatstability test of WROBLEWSKI and GREGORY (1961), as described by PAVEL (1967), was performed by heating the homogenates at 57" C and 65" C for 30 minutes, after which the remaining enzymatic activity was compared with that of an unheated sample.…”

Section: Methodsmentioning

confidence: 99%

Changes in Lactate Dehydrogenase Isoenzymes of Liver, Heart and Skeletal Muscles of the Pig*

Hende

Muylle

Oyaert

2010

Zentralblatt Für Veterinärmedizin Reihe A

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Summary Electrophoretic separation of LDH isoenzymes was compared with substrate specificity tests and thermal stability tests of homogenates of liver, heart and skeletal muscle of pigs of different ages. In heart muscle the greatest activity was found in LDH1, little activity in LDH2 and only traces of activity in LDH3. The BDH/LDH quotient was relatively high (0.66–0.88). In the liver of young animals the bulk of the activity was found in LDH1 and LDH2; with ageing this pattern changed to a mainly LDH3 pattern, with gradually diminishing% activity after heating at 65° C. After electrophoresis of LDH isoenzymes of the skeletal muscle of baby pigs, most of the activity was found in the LDH5 fraction and little in the four other fractions which disappear with ageing. The ratio BDH/LDH also diminished gradually with ageing. Zusammenfassung Veränderungen der Lactat‐Dehydrogenase‐Isoenzyme der Leber sowie des Herz‐ und Skelettmuskels des Schweines Elektrophoretisch getrennte Lactat‐Dehydrogenase‐Isoenzyme von Leberhomogenaten, Herz‐ und Skelettmuskeln der Schweine wurden auf ihre Substrat‐Spezifität und Hitzestabilität geprüft. Der Herzmuskel wies die größte LDH1‐Aktivität auf, während die Aktivität der LDH2 klein und diejenige von LDH3 äußerst gering waren. Der BDH/LDH‐Quotient (Butynat/Lactat) war relativ hoch (0,66–0,88). In der Leber von Jungtieren machten die LDH1 und LDH2 die Hauptaktivität aus, mit dem Älterwerden der Tiere erreichte die LDH3 die größte Aktivität. Eine Erhitzung der Proben auf 65° C führte zu einem fast vollständigen Verlust der Fermentaktivität. Bei elektrophoretisch gewonnenen LDH‐Isoenzymen aus dem Skelettmuskel von neugeborenen Ferkeln zeigte die LDH5 die größte Aktivität, während die vier andern Enzymfraktionen nur geringe Aktivitäten aufwiesen; welche zudem mit dem Altern der Tiere verschwanden. Der Aktivitätsquotient BDH/LDH wurde mit dem Älterwerden der Tiere sukzessive kleiner. Résumé Modification des isoenzymes de la déhydrogénase lactique du foie, du coeur et des muscles du squlette chez le porc On compare la séparation électrophorétique des isoenzymes LDH avec les tests de spécificité du substrat et les tests de stabilité thermique des homogénats de foie, de coeur et de muscles du squelette chez des porcs à différents âges. Dans le muscle cardiaque, on trouve l'activité la plus forte du LDH1, une faible activité du LDH2 et seulement des traces d'activité du LDH3. Le quotient BDH/LDH est relativement élevé (0,66–0,88). Dans le foie des jeunes animaux, le maximum de l'activité se trouve chez les LDH3, et LDH2; avec l'âge, cet état change en une domination de LDH3, avec un pourcentage d'activité diminuant graduellement après chauffage à 65° C. Après électrophorèse des isoenzymes LDH des muscles du squelette des porcelets, la plus forte activité se trouve dans la fraction des LDH5. Le peu que l'on trouve dans les quatre autres fractions disparaît avec l'âge. Le rapport BDH/LDH diminue aussi graduellement avec l'âge. Resumen Cambios en los isoenzimas lactatodehidrogenásicos del hígado, ...

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“…The use of cold buffer and the short migration time prevented inactivation of the labile LDH-4 and LDH-5. Color development according to the sandwich technique of Barnett [8,9] was accomplished more simply by enclosing the electrophoretic strip and the substrate strip between glass slides [13]. This prevented curling of the cellulose acetate.…”

Section: Comments To the Methodsmentioning

confidence: 99%

“…51107} impregnated with a substrate and staining mixture according to a modification of the procedure described by Barnett [8,9].…”

Section: Detection Of Tile Ldh-isoenzymesmentioning

confidence: 99%

The behaviour of LDH-3 in patients with malignant diseases during therapy with cytostatic drugs and prednisone, studied by LDH-isoenzyme electrophoresis on cellulose acetate

Gennip

Gorcum

Taminiau

et al. 1975

Clinica Chimica Acta

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SummaryA modified method used for the quantitative estimation of LDH-isoenzymes in serum after electrophoresis on c~llulose acetate is described.Total LDH-activit~ and isoenzyme distribution in serum samples of capillary blood are compared to those in samples collected by venipuncture.Total LDH-values and Lt)H-distributions both in 2c' normal children and 14 children with maii~.o~.-,t ~_ise,~es aze given.:~'nen studying the LDH

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Dehydrogenase Isoenzymes

Cited by 24 publications

References 2 publications

Quantitative Determinations of Serum Lactate Dehydrogenase Isoenzymes in Cases of Antepartum Haemorrhage

Quantitative Determinations of Serum Lactate Dehydrogenase Isoenzymes in Cases of Antepartum Haemorrhage

Changes in Lactate Dehydrogenase Isoenzymes of Liver, Heart and Skeletal Muscles of the Pig*

The behaviour of LDH-3 in patients with malignant diseases during therapy with cytostatic drugs and prednisone, studied by LDH-isoenzyme electrophoresis on cellulose acetate

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