scholarly journals Examination of the Protein Composition of the Cell Envelope of Escherichia coli by Polyacrylamide Gel Electrophoresis

1970 ◽  
Vol 104 (2) ◽  
pp. 882-889 ◽  
Author(s):  
Carl A. Schnaitman
1976 ◽  
Vol 22 (2) ◽  
pp. 309-312 ◽  
Author(s):  
R. R. B. Russell ◽  
I. J. McDonald

In an attempt to elucidate the relation between Micrococcus cryophilus, Neisseria caviae, Neisseria ovis, and Branhamella catarrhalis, fractions derived from outer membranes of a strain of each organism were examined for protein composition by SDS – polyacrylamide gel electrophoresis. Micrococcus cryophilus outer membrane protein showed extensive similarities to that of N. ovis and contained a heat-modifiable protein which behaved almost identically with the corresponding bands previously shown to exist in N. caviae and N. oris. Branhamella catarrhalis protein was distinctly different from those of M. cryophilus and the two 'false neisserias' N. caviae and N. oris.


1974 ◽  
Vol 143 (3) ◽  
pp. 607-612 ◽  
Author(s):  
Graham Moore ◽  
Robert R. Crichton

Escherichia coli ribosomes were treated with a number of different aldehydes of various sizes in the presence of NaBH4. After incorporation of either 3H or 14C, the ribosomal proteins were separated by two-dimensional polyacrylamide-gel electrophoresis and the extent of alkylation of the lysine residues in each protein was measured. The same pattern of alkylation was observed with the four reagents used, namely formaldehyde, acetone, benzaldehyde and 3,4,5-trimethoxybenzaldehyde. Every protein in 30S and 50S subunits was modified, although there was considerable variation in the degree of alkylation of individual proteins. A topographical classification of ribosomal proteins is presented, based on the degree of exposure of lysine residues. The data indicate that every protein of the ribosome has at least one lysine residue exposed at or near the surface of the ribonucleo-protein complex.


1990 ◽  
Vol 68 (5) ◽  
pp. 895-900 ◽  
Author(s):  
Thomas Olin ◽  
Alexandra von der Decken

The developmental stages of oocytes, eyed eggs, and alevins from salmon (Salmo salar) were compared for their yolk protein composition. In oocytes, SDS–polyacrylamide gel electrophoresis showed high amounts of a protein with the molecular weight (Mr) of 94 000. In eyed eggs, the 94 000 protein decreased and was undetectable in the alevins. Furthermore, in eyed eggs the proteins of 67 000, 30 000, and 27 000 increased, while in the alevins the concentration of the 67 000 protein decreased and that of the 39 000 increased. Vitellogenin-specific antigen sites analyzed by immunoblotting were most pronounced with the proteins of 94 000, 67 000, 39 000, 30 000, 23 000, and 19 000. Separation of the yolk proteins by HPLC gave four peaks at 280 nm for all three developmental stages. Each peak consisted of several proteins as analyzed by SDS–polyacrylamide gel electrophoresis. The 7-day-old alevins sampled from groups of different parental origin showed differences in the amount of the 67 000 and 23 000 proteins. Expectancy of survival within the group in connection with a slow disappearance of the 67 000 and 23 000 proteins was statistically significant. A fast disappearance may be used as an indication of, but not as the reason for, a high mortality within one group of alevins.


1971 ◽  
Vol 49 (8) ◽  
pp. 1293-1297 ◽  
Author(s):  
Gilles Pelletier ◽  
Robert Hall

Buffer-soluble proteins extracted from six morphologically different isolates of Verticillium were separated by polyacrylamide gel-electrophoresis. Protein patterns from the six isolates were different from one another whether extracts were prepared from conidia, from young colonies composed of mycelium and conidia, or from 6-day-old mycelium. However, the nature of the patterns, and therefore the degree of differences among species patterns, was influenced by the types of cells from which the extracts were prepared.Patterns of proteins from V. tricorpus, V. nigrescens, and an isolate of uncertain identity (isolate 2) which produced chlamydospores and dark mycelium were clearly different from one another whether extracts were prepared from conidia or mycelium. In contrast, conidia of V. albo-atrum, of V. dahliae, and of an isolate which did not produce pigmented structures produced very similar patterns which differed by only a few protein bands. This close similarity of patterns supports the view that V. albo-atrum and V. dahliae are genetically closely related.The protein composition of conidia differed from that of mycelium. In V. albo-atrum, spore extracts contained at least three proteins not detected in mycelium extracts. Differences between spores and mycelium were even greater in V. nigrescens and isolate 2. Analysis of V. dahliae showed differences between spores, 3-day-old mycelium, and 6-day-old mycelium.Our results support the view that gel-electrophoresis of proteins is useful as a taxonomic tool provided attention is given to the degree of morphological differentiation of the materials to be compared.


1983 ◽  
Vol 213 (1) ◽  
pp. 187-191 ◽  
Author(s):  
A Lewendon ◽  
J R Coggins

A procedure for the purification of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli is described. Homogeneous enzyme of specific activity 17.7 units/mg was obtained in 22% yield. The key purification step involves substrate elution of the enzyme from a cellulose phosphate column. The subunit Mr was estimated to be 49 000 by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. The native Mr was estimated to be 55 000 by gel filtration, indicating that the enzyme is monomeric.


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