scholarly journals Multiple growth-associated nuclear proteins immunoprecipitated by antisera raised against human c-myc peptide antigens.

1986 ◽  
Vol 6 (3) ◽  
pp. 942-949 ◽  
Author(s):  
H Persson ◽  
H E Gray ◽  
F Godeau ◽  
S Braunhut ◽  
A R Bellvé
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Nuclear Localization ◽  
Cell Nucleus ◽  
Sodium Dodecyl ◽  
Nuclear Proteins ◽  
Immunofluorescent Staining ◽  
Nuclear Staining ◽  
Polyacrylamide Gels ◽  
Peptide Antigens ◽  
Molecular Masses

Different antisera raised against various regions of the human c-myc protein were used to identify four human c-myc proteins with apparent molecular masses in sodium dodecyl sulfate-polyacrylamide gels ranging from 64 to 68 kilodaltons (phosphoproteins pp64 and pp67 and nonphosphorylated proteins p65 and p68). pp64 and p65 were the major detectable c-myc proteins, and pp67 and p68 were minor but specific components of the immunoprecipitates. The c-myc proteins were all localized in the cell nucleus. Accumulation of [35S]methionine-labeled p65 was observed after pulse-labeling and chase, suggesting that the stable p65 c-myc protein is generated posttranslationally from short-lived precursors. pp64, pp67, and p68 possessed short half-lives and may therefore be precursors of the stable p65. Confirmation of the nuclear localization of the human c-myc proteins was obtained by immunofluorescent staining. The human c-myc proteins were revealed as a pattern of punctate nuclear staining with, particularly for p65, nucleolar enhancement that left an unstained annulus surrounding the nucleolus.

Multiple growth-associated nuclear proteins immunoprecipitated by antisera raised against human c-myc peptide antigens

1986 ◽  
Vol 6 (3) ◽  
pp. 942-949
Author(s):  
H Persson ◽  
H E Gray ◽  
F Godeau ◽  
S Braunhut ◽  
A R Bellvé
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Nuclear Localization ◽  
Cell Nucleus ◽  
Sodium Dodecyl ◽  
Nuclear Proteins ◽  
Immunofluorescent Staining ◽  
Nuclear Staining ◽  
Polyacrylamide Gels ◽  
Peptide Antigens ◽  
Molecular Masses

Different antisera raised against various regions of the human c-myc protein were used to identify four human c-myc proteins with apparent molecular masses in sodium dodecyl sulfate-polyacrylamide gels ranging from 64 to 68 kilodaltons (phosphoproteins pp64 and pp67 and nonphosphorylated proteins p65 and p68). pp64 and p65 were the major detectable c-myc proteins, and pp67 and p68 were minor but specific components of the immunoprecipitates. The c-myc proteins were all localized in the cell nucleus. Accumulation of [35S]methionine-labeled p65 was observed after pulse-labeling and chase, suggesting that the stable p65 c-myc protein is generated posttranslationally from short-lived precursors. pp64, pp67, and p68 possessed short half-lives and may therefore be precursors of the stable p65. Confirmation of the nuclear localization of the human c-myc proteins was obtained by immunofluorescent staining. The human c-myc proteins were revealed as a pattern of punctate nuclear staining with, particularly for p65, nucleolar enhancement that left an unstained annulus surrounding the nucleolus.

Ubiquitin immunoreactivity shows several proteins varying with development and sporulation in the basidiomycete Coprinus cinereus

1990 ◽  
Vol 68 (7-8) ◽  
pp. 1019-1025 ◽  
Author(s):  
Tosaku Kanda ◽  
Nobuharu Tanaka ◽  
Tsuneo Takemaru
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Light Period ◽  
Coprinus Cinereus ◽  
Polyacrylamide Gels ◽  
Wild Type ◽  
Stages Of Development ◽  
Crude Extracts ◽  
Dodecyl Sulfate ◽  
Molecular Masses

Crude extracts of mycelia and basidiocarp primordia in the basidiomycete Coprinus cinereus were resolved on sodium dodecyl sulfate – polyacrylamide gels, and ubiquitin and several proteins were detected by immunoblotting with anti-ubiquitin antibody. The molecular masses of the proteins detected were 30 900, 28 600, 27 800, 26 300, 22 500, and 15 400 daltons, respectively. Relative levels of ubiquitin and the ubiquitin-immunoreactive proteins were measured in different stages of development. The levels of ubiquitin and most of the ubiquitin-immunoreactive proteins in basidiocarp primordium formation increased and in basidiocarp maturation decreased in cap and upper stipe, while in lower stipe became high except for the 27 800 dalton protein and ubiquitin. During sporulation, ubiquitin and all the ubiquitin-immunoreactive proteins tended to decrease in the cap of the young wild-type basidiocarp. The levels of 30 900 and 15 400 dalton proteins increased transiently at 6–10 h after the beginning of the last light period, while ubiquitin decreased markedly. No correlation was observed between changes in levels of the ubiquitin-immunoreactive proteins and the blocked stages in sporulation-deficient mutants.Key words: ubiquitin, development, sporulation, Coprinus.

Efficacy and compatibility with mass spectrometry of methods for elution of proteins from sodium dodecyl sulfate–polyacrylamide gels and polyvinyldifluoride membranes

2004 ◽  
Vol 330 (1) ◽  
pp. 87-97 ◽  
Author(s):  
Charlotte Sværke Jørgensen ◽  
Mitchell Jagd ◽  
Birgitte Kjær Sørensen ◽  
Jim McGuire ◽  
Vibeke Barkholt ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gels ◽  
Dodecyl Sulfate

scholarly journals Transformation-deficient mutants of Bacillus subtilis impaired in competence-specific nuclease activities

1982 ◽  
Vol 152 (1) ◽  
pp. 166-174
Author(s):  
J A Mulder ◽  
G Venema
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Magnesium Ions ◽  
Polyacrylamide Gels ◽  
Wild Type ◽  
Molecular Weights ◽  
Defective Mutant ◽  
Mutant Strains

A comparison of the nucleolytic activities in competent and physiologically low-competent wild-type cultures of Bacillus subtilis in DNA-containing sodium dodecyl sulfate-polyacrylamide gels revealed the existence of three competence-associated nuclease activities with apparent molecular weights of 13,000, 15,000, and 26,000. The three activities, which were dependent on manganese or magnesium ions, were specifically present in the competent fraction of a competent culture. The competence-associated nucleolytic activities of eight transformation-defective mutant strains were assayed, resulting in the following three classes of mutants: (i) four strains which, according to this assay, were not impaired in any of the nucleolytic activities mentioned above; (ii) one strain which was strongly impaired in the 13,000- and 26,000-molecular-weight activities, but showed a considerable level of the 15,000-molecular-weight activity; and (iii) three strains which were severely impaired in all three activities. The results indicated that the 26,000-molecular-weight activity was a dimer of the 13,000-molecular-weight activity and that this nuclease was involved in the entry of DNA.

Detection of N-glycans on small amounts of glycoproteins in tissue samples and sodium dodecyl sulfate–polyacrylamide gels

2012 ◽  
Vol 423 (2) ◽  
pp. 253-260 ◽  
Author(s):  
Takeshi Yoshimura ◽  
Gen Yamada ◽  
Mai Narumi ◽  
Takako Koike ◽  
Akihiro Ishii ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gels ◽  
Tissue Samples ◽  
Dodecyl Sulfate
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