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Digitale Medien

Configuration of unsheared nucleohistone. Effects of ionic strength and of histone F1 removal (1976)

Lewis, Edwin A. ; DeBuysere, Michael S. ; Rees, Allan W.

s.l. : American Chemical Society

Biochemistry 15 (1976), S. 186-192

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ISSN: 1520-4995

Quelle: ACS Legacy Archives

Thema: Biologie , Chemie und Pharmazie

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1021/bi00646a029

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Digitale Medien

Size determination of multienzyme complexes using two-dimensional agarose gel electrophoresis (1989)

Easom, Richard A. ; Debuysere, Michael S. ; Olson, Merle S. ; [weitere]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 5 (1989), S. 224-232

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ISSN: 0887-3585

Schlagwort(e): effective pore's radius ; α-ketoglutarate dehydrogenase complex ; branched chain α-keto acid dehydrogenase complex ; electron microscopy ; multienzyme complex ; two-dimensional ; electrophoresis ; multienzyme complex ; aggregation of Pyruvate dehydrogenase complex ; Chemistry ; Biochemistry and Biotechnology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Medizin

Notizen: In the studies of the size and structure of multienzyme complexes, a procedure complementary to electron microscopy for determining the molecular dimensions of hydrated multisubunit complexes is needed. For some applications this procedure must be capable of detecting aggregation of complexes and must be applicable to impure preparations. In the present study, a procedure of two-dimensional agarose gel electrophoresis (2d-AGE) (Serwer, P. et al. Anal. Biochem. 152: 339-345, 1986) was modified and employed to provide accurate sizemeasurements of several classical multienzyme complexes. To improve band clarity and to achieve required gel pore sizes, a hydroxyethylated agarose was used. The effective pore's radius (PE) as a function of gel concentration was determined for this agarose inthe range of PE value needed for multienzyme complexes (effective radius, R = 10-30 nm). Appropriate conditions wereestablished to measure R value ± 1% of the pyruvate (PDC), α-ketoglutarate (α-KGDC), and the branched chain α-keto acid (BCDC) dehydrogenase multienzyme complexes; the accuracy of R was limited by the accuracy of the determinations of the R value for the sizestandards. The PDC from bovine heart was found to have an R = 22.4 ± 0.2 nm following cross-linking with glutaraldehyde that was necessary for stabilization of the complex. Dimers and trimers of PDC, present in the preparations used, were separated from monomeric PDCduring 2d-AGE. All R values for the enzyme complexes studied were agreement with, though more accurate than, R valuesobtained by use of electron microscopy. In contrast to this statement, the internal dihydrolipoyl transacetylase core of PDC (E2) had an R of 18.8 ± 0.2 nm using 2d-AGE, but 10.5 nm by electron microscopy. This observation confirms the proposal that the core of the PDC has externally projecting fibrous domains invisibleto electron microscopy.

Zusätzliches Material: 7 Ill.