Relationships among species of Verticillium: protein composition of spores and mycelium

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.

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.


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