Protein analysis in a pleomorphically deteriorated strain of the insect-pathogenic fungus Metarhizium anisopliae

2002 ◽  
Vol 48 (9) ◽  
pp. 787-792 ◽  
Author(s):  
Andrena M Kamp ◽  
Michael J Bidochka

Pleomorphic deterioration is a process where a fungal isolate loses the ability to produce conidia during repeated subculturing. We have previously isolated strains of the entomopathogenic fungus Metarhizium anisopliae that have irreversibly lost the ability to produce conidia and only produce mycelia when grown on agar. Gel electrophoresis was used to examine differences in intracellular protein patterns (urea-soluble proteins and urea-insoluble proteins (i.e., hydrophobins)) in conidiating and mycelial cultures of M. anisopliae. Two major proteins present in a conidiating culture and one from a mycelial culture were N-terminally sequenced but showed no homologies to known proteins. The presence of hydrophobins in conidiating and mycelial cultures was also examined, and it was shown that these proteins were abundant in conidiating cultures but not in mycelial cultures. We also used primers designed from regulatory genes involved in conidiation in Aspergillus nidulans. The amplified fragments were not homologous to A. nidulans genes.Key words: Metarhizium anisopliae, conidia, pleomorphic deterioration, protein analysis.

1964 ◽  
Vol 10 (1) ◽  
pp. 62-68 ◽  
Author(s):  
Tatsuo Hase

Abstract A simple microelectrophoretic method of protein analysis using the gel of starch agar mixture is described. The method is easily standardized and the results show consistency and reproducibility. Protein patterns obtained show higher resolution than those of paper or agar-gel electrophoresis and simulate that of starch-gel electrophoresis. Developed protein patterns are suitable to quantitative analysis by appropriate electrophotometric or ultraviolet-light scanning devices and can be preserved as permanent records.


The Lancet ◽  
1974 ◽  
Vol 304 (7892) ◽  
pp. 1321-1322
Author(s):  
W.H. Taylor ◽  
D.J. Etherington

Blood ◽  
1965 ◽  
Vol 25 (5) ◽  
pp. 830-838 ◽  
Author(s):  
VIRGINIA MINNICH ◽  
ROBERT J. HILL ◽  
PHILIP D. KHURI ◽  
MARY E. ANDERSON

Abstract A new hemoglobin, hemoglobin Hope, with a beta chain abnormality has been found in three generations of a St. Louis Negro family. The abnormal hemoglobin in the heterozygous state caused neither clinical stigmata nor abnormality in the red blood cells. Hemoglobin Hope was detected by agar gel electrophoresis at pH 6.2, but could not be differentiated from hemoglobin A by starch block electrophoresis at pH 8.6. Also, it could not be separated from hemoglobin A by paper, or starch gel electrophoresis employing a range of buffers from pH 6.2 to 8.6. Amino acid analysis showed that aspartic acid was substituted for glycine at position 136 of the beta chain. Hemoglobin Hope may be formulated as α2Aβ2136 gly-asp.


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