The effects of temperature on the growth and polypeptide composition of several snow mold species

1985 ◽  
Vol 63 (12) ◽  
pp. 2311-2318 ◽  
Author(s):  
W. J. Newsted ◽  
N. P. A. Huner ◽  
J. P. Insell ◽  
M. Griffith ◽  
R. B. van Huystee
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Vegetative Growth ◽  
Gel Electrophoresis ◽  
Agar Medium ◽  
Polyacrylamide Gel Electrophoresis ◽  
Relative Proportion ◽  
Sodium Dodecyl ◽  
Polypeptide Composition ◽  
Effects Of Temperature ◽  
Typhula Incarnata

Myriosclerotinia borealis (W51), Coprinus spp. (13W1 and 14W2), Typhula idahoensis (W21), and Typhula incarnata (W29) were incubated in the dark on a defined agar medium at permissive (4 °C) and nonpermissive temperatures (22 and 30 °C). Isolates of Coprinus spp. and Typhula spp. required higher temperatures than M. borealis to arrest vegetative growth completely. The effects of incubation at permissive and nonpermissive temperatures on the polypeptide compositions of M. borealis, Coprinus spp., T. idahoensis (W21), and T. incarnata (W29) were examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The results indicated that the number of polypeptides in the polypeptide complement of M. borealis and both Typhula species decreased significantly during incubation at nonpermissive temperatures. In contrast, Coprinus sp. (13W1) showed no significant change in the number of polypeptides observed during incubation at nonpermissive temperatures. Furthermore, there appeared to be an increase in the relative proportion of at least three polypeptides during incubation of Coprinus at nonpermissive temperatures. The significance of these species-dependent responses to nonpermissive growth temperatures is discussed.

Light microscopic and polypeptide analyses of sclerotia from mesophilic and psychrophilic pathogenic fungi

1985 ◽  
Vol 63 (12) ◽  
pp. 2305-2310 ◽  
Author(s):  
James P. Insell ◽  
N. P. A. Huner ◽  
W. Jay Newsted ◽  
R. B. van Huystee
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sclerotium Rolfsii ◽  
Pathogenic Fungi ◽  
Polypeptide Composition ◽  
Thin Walled ◽  
Hard Structures ◽  
A Minor

The structure and polypeptide composition of sclerotia of three mesophilic pathogenic fungi, Sclerotinia sclerotiorum, Sclerotium rolfsii, and Botrytis cinerea, and one psychrophilic snow mold, Myriosclerotinia borealis, were compared. The sclerotia of S. sclerotiorum and B. cinerea were black, round, hard structures which were composed of three areas: the rind, the cortex, and the medulla. Both the cortical and medullary areas of these sclerotia exhibited intensely stained inclusions. In contrast, sclerotia of M. borealis were not present as discrete entities but coalesced near the central point of inoculation. These black sclerotial masses were composed of thin-walled, pseudoparenchymal cells tightly packed together to form two distinct areas: a rind and a medullarylike region. No inclusions were evident in the medulla of cells of M. borealis sclerotia. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of sclerotial extracts of mesophilic fungi indicated the presence of major polypeptides. The polypeptide complement of B. cinerea contained a single, major polypeptide with an apparent molecular mass of 33 to 36 kDa. Similarly, sclerotia of S. sclerotiorum contained one major polypeptide of approximately 36 kDa in addition to one minor polypeptide of about 18 kDa. However, sclerotia of S. rolfsii contained a major polypeptide of about 16 kDa. Sclerotia of M. borealis contained a major polypeptide of 32 to 36 kDa and a minor polypeptide of about 16 kDa.

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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