A survey on the formation and localization of secondary isozymes in mammalia

Rothe, Gunter M.

doi:10.1007/bf00295687

Cited by 12 publications

References 191 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Determination of molecular weights and Stokes' radii of non‐denatured proteins by polyacrylamide gradient gel electrophoresis. 2. Determination of the size of stable and labile molecular weight variants of enzymes from plant sources

Rothe

Purkhanbaba

1982

Electrophoresis

Self Cite

View full text Add to dashboard Cite

weight variants of enzymes from plant sourcesUnder certain conditions in polyacrylamide gradient gel electrophoresis (PAGGE), a linear correlation between the logarithm of the size of calibration proteins (log MW or log RJ and the square root of their migration distance (m) can be observed; slope and intercept of the calibration curve depend on the duration of electrophoresis; linearity, however, is maintained over a wide range (4-60 h, 200 V) (Rothe and Purkhanbaba, Electrophoresis 1982,3,33-42.) Using this method the reaction of plant isozyme systems penetrating a linear polyacrylamide (PAA) gradient gel was investigated: lactate dehydrogenase (LDH) from potato tubers behaves similarly to animal calibration proteins. The enzyme exhibits 3 subbands with molecular weights of 144 000, 150 000 and 156 000 (+ 1.7 %), respectively. The enzyme system "shikimate oxidoreductase" (SORase) behaves significantly different: during PAGGE it splits into 2 major bands (-60 000 and -1 10 000, respectively) consisting of several subbands. The results of our experiments show that SORase is present in vivo as a complex system. We believe that this complex is partly indentical with the so-called pre-chorismate complex.

show abstract

Determination of molecular weights and Stokes' radii of non‐denatured proteins by polyacrylamide gradient gel electrophoresis. 2. Determination of the size of stable and labile molecular weight variants of enzymes from plant sources

Rothe

Purkhanbaba

1982

Electrophoresis

Self Cite

View full text Add to dashboard Cite

show abstract

Determination of molecular weights and Stokes' radii of non‐denatured proteins by polyacrylamide gradient gel electrophoresis 3. Estimation of the upper and lower size limits of carbonic anhydrase as a model for complexing enzymes

1985

View full text Add to dashboard Cite

Determination of molecular weights and Stokes' radii of non-denatured proteins by polyacrylamide gradient gel electrophoresis 3. Estimation of the upper and lower size limits of carbonic anhydrase as a model for complexing enzymesStudying the separation behavior of various native carbonic anhydrase isozymes from mammalian erythrocytes we found that the migration of these enzymes differs from that of the marker proteins commonly used in gradient gel electrophoresis. In alkaline buffer systems the enzymes from human, bovine, rabbit, and canine erythrocytes start to migrate with a size apparently 6 to 12 times larger than their monomeric size, then gradually lose in apparent size and finally end up in a size equivalent to their monomeric mol mass. We determined the monomeric mol mass of the various carbonic anhydrase forms to be 23 000 to 39 000 (g/mol). These values are in accordance with different data in the literature and the data which we obtained by sodium dodecyl sulfate-gradient gel electrophoresis. The equations and the graphical solutions needed to calculate the apparent upper size as well as the monomeric size of mammalian carbonic anhydrases are presented. It is demonstrated by this example that only the time-dependent version of non-denaturing polyacrylamide giadient gel electrophoresis provides reliable mol mass estimations.

show abstract

Epigenetic modification of murine Cu,Zn‐superoxide dismutase

Shibata

Ogita

1986

Electrophoresis

View full text Add to dashboard Cite

,Zn-superoxide dismutase (SOD) from erythrocytes has three isozymes, SOD-1A (pZ 6.4), B (pZ 5.7) and C (pZ5.0). It has been suggested that SOD-1A is formed epigenetically by asymmetric modification of SOD-1B where as SOD-1C is produced by treatment of superoxide dismutase with hydrogen peroxide. On twodimensional gel electrophoretic analysis, each isozyme shows two forms, easily permuted into each other, and hence supposed to be in equilibrium. The zymogram patterns of murine liver, kidney, heart and brain are the same as those in erythrocytes although SOD activity levels are different in these tissues.

show abstract

A survey on the formation and localization of secondary isozymes in mammalia

Cited by 12 publications

References 191 publications

Determination of molecular weights and Stokes' radii of non‐denatured proteins by polyacrylamide gradient gel electrophoresis. 2. Determination of the size of stable and labile molecular weight variants of enzymes from plant sources

Determination of molecular weights and Stokes' radii of non‐denatured proteins by polyacrylamide gradient gel electrophoresis. 2. Determination of the size of stable and labile molecular weight variants of enzymes from plant sources

Determination of molecular weights and Stokes' radii of non‐denatured proteins by polyacrylamide gradient gel electrophoresis 3. Estimation of the upper and lower size limits of carbonic anhydrase as a model for complexing enzymes

Epigenetic modification of murine Cu,Zn‐superoxide dismutase

Contact Info

Product

Resources

About