ZONE ELECTROPHORESIS OF CALF THYMUS HISTONE IN STARCH GEL

1960 ◽  
Vol 38 (1) ◽  
pp. 355-363 ◽  
Author(s):  
J. M. Neelin ◽  
E. M. Neelin
Keyword(s):  
Amino Acids ◽  
Gel Electrophoresis ◽  
Low Ph ◽  
Acid Extraction ◽  
Starch Gel Electrophoresis ◽  
Calf Thymus ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Terminal Amino

A total of 19 zones were detected by starch gel electrophoresis of calf thymus histone in buffers of 0.02 μ below pH 5.0. Of these, 18 were evident at pH 4.9 (acetate) and 15 at pH 3.9 (formate). Above pH 5.0, aggregation interfered with resolution, but by adding 4 M urea to the gel sufficient resolution was obtained between pH 4.4 and 8.7 to distinguish a total of 22 zones. Of this total, three fast components were present only occasionally in trace amounts, and three others were resolved from the immobile aggregated histone at low pH only. At least 16 zones appeared to be native histone components. Acid extraction of the histone did not appear to cause degradation since no new N-terminal amino acids were generated by this step. Two different methods of preparation produced histone extracts with essentially the same electrophoretic properties.

ZONE ELECTROPHORESIS OF CALF THYMUS HISTONE IN STARCH GEL

1960 ◽  
Vol 38 (4) ◽  
pp. 355-363 ◽  
Author(s):  
J. M. Neelin ◽  
E. M. Neelin
Keyword(s):  
Amino Acids ◽  
Gel Electrophoresis ◽  
Low Ph ◽  
Acid Extraction ◽  
Starch Gel Electrophoresis ◽  
Calf Thymus ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Terminal Amino

A total of 19 zones were detected by starch gel electrophoresis of calf thymus histone in buffers of 0.02 μ below pH 5.0. Of these, 18 were evident at pH 4.9 (acetate) and 15 at pH 3.9 (formate). Above pH 5.0, aggregation interfered with resolution, but by adding 4 M urea to the gel sufficient resolution was obtained between pH 4.4 and 8.7 to distinguish a total of 22 zones. Of this total, three fast components were present only occasionally in trace amounts, and three others were resolved from the immobile aggregated histone at low pH only. At least 16 zones appeared to be native histone components. Acid extraction of the histone did not appear to cause degradation since no new N-terminal amino acids were generated by this step. Two different methods of preparation produced histone extracts with essentially the same electrophoretic properties.

Comparative zone electrophoresis of catalase of Staphylococcus species isolated from mammalian skin

1976 ◽  
Vol 22 (12) ◽  
pp. 1691-1698 ◽  
Author(s):  
Raymond J. Zimmerman
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Polyacrylamide Electrophoresis ◽  
Electrophoretic Mobilities ◽  
Mammalian Skin ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Molecular Sieving

Vertical polyacrylamide slab gel electrophoresis was conducted for the catalase enzymes of representative strains of 18 proposed species and subspecies of the genus Staphylococcus. The catalase bands which resulted were predominantly monomorphic within each of the species and differences in catalase mobilities were observed between many of the species. The electrophoretic mobilities of the catalases were supportive to the scheme of classification used. Many strains of certain species demonstrated multiple catalase bands which are suggestive of multimolecular forms of the enzyme. Horizontal starch gel electrophoresis of representative strains of S. capitis produced catalase bands with relative mobilities that were different from those obtained with polyacrylamide electrophoresis, presumably due to a difference in molecular sieving between the gels.

A COMPARISON OF HISTONES FROM CHICKEN TISSUES BY ZONE ELECTROPHORESIS IN STARCH GEL

1961 ◽  
Vol 39 (3) ◽  
pp. 485-491 ◽  
Author(s):  
J. M. Neelin ◽  
G. C. Butler
Keyword(s):  
Cell Differentiation ◽  
Ionic Strength ◽  
Gel Electrophoresis ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Chicken Erythrocytes ◽  
Characteristic Zone

Histories were extracted at pH 1.7 from washed nuclei of chicken erythrocytes, spleen, liver, and testis and compared by starch-gel electrophoresis at pH 5.0, ionic strength 0.020. Spleen and liver histories displayed the most complex electrophoretic patterns with 18 zones each and differed only in relative proportions of certain zones. Erythrocyte histone contained a characteristic zone while lacking a group present in spleen and liver histones. Testis histone with only seven zones differed markedly from the other three. These results were consistent with chromatograms of erythrocyte, spleen, and liver histones on sodium IRC-50. The suggested correlation of tissue-specific histones with cell differentiation is discussed.

The tertiary phase of rennin action on αs- and β-caseins

1970 ◽  
Vol 37 (3) ◽  
pp. 437-444 ◽  
Author(s):  
A. M. El-Negoumy
Keyword(s):  
Amino Acid ◽  
Degradation Product ◽  
Gel Electrophoresis ◽  
Phosphate Buffer ◽  
Starch Gel Electrophoresis ◽  
Terminal Amino Acid ◽  
Starch Gel ◽  
Terminal Amino

SummaryCasein, whole αs-casein and β-casein were incubated for 3 and 14 h with crystalline rennin, at pH 6·60 and 36 °C, both in phosphate buffer and in milk dialysate. Products obtained from both systems, comprising 30–83% calciumsensitive (Cas) components, gave similar patterns on starch gel electrophoresis. Whole casein and whole αs-casein were not so soluble in milk dialysate as in phosphate buffer. No significant differences in composition were observed between the Cas and the calcium-insensitive (Ca1) products from the same source.The αs1-component of the Cas product from rennin-treated whole αs-casein had faster gel mobility in comparison to the αs1-component in the Cas product from untreated whole αs-casein. Also, αs1-casein yielded one faster-moving degradation product, while αs2,3,4 appeared unaltered after 14h. The Cas product of rennintreated β-casein also had faster mobility than untreated β-casein and yielded one faster degradation product and several minor ones of slower mobility. Arginine was the only N-terminal amino acid found in the Cas product of both rennin-treated and untreated αs - and β-caseins. The arginine content increased from 3·48 and 4·98 moles/105g to 5·12 and 6·38 moles/105g in the Cas products from rennin-treated β-and αs-caseins, respectively.

CHARACTERIZATION OF THE ESTERASES FROM ELECTRIC TISSUE OF ELECTROPHORUS BY STARCH-GEL ELECTROPHORESIS

1967 ◽  
Vol 45 (7) ◽  
pp. 1099-1105 ◽  
Author(s):  
D. J. Ecobichon ◽  
Y. Israel
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Electrophorus Electricus ◽  
Vertical Zone ◽  
Zone Electrophoresis ◽  
Starch Gel

The water-soluble esterases of a microsome-free supernatant of the electric tissue of Electrophorus electricus were separated by vertical-zone electrophoresis in starch gel. Specific and nonspecific substrates and inhibitors were used in conjunction with histochemical techniques to identify the enzymes. Acetylcholinesterase was present in the form of four bands of activity, the electrophoretic mobility of which was suggestive of aggregated forms of the enzyme. Pseudocholinesterase was detected as two weak bands of activity. A third esterase was identified as a nonspecific carboxylesterase and shown to be a sialoprotein.

scholarly journals CHARACTERISTICS OF STREPTOCOCCAL GROUP-SPECIFIC ANTIBODY ISOLATED FROM HYPERIMMUNE RABBITS

1966 ◽  
Vol 123 (4) ◽  
pp. 599-614 ◽  
Author(s):  
C. Kirk Osterland ◽  
Edward J. Miller ◽  
Walter W. Karakawa ◽  
Richard M. Krause
Keyword(s):  
New Zealand ◽  
Specific Antibody ◽  
Gel Electrophoresis ◽  
Limited Range ◽  
Carbohydrate Antigen ◽  
Starch Gel Electrophoresis ◽  
Normal Complement ◽  
Zone Electrophoresis ◽  
Group A ◽  
Starch Gel

Intravenous immunization of New Zealand red rabbits with streptococcal group-specific bacterial vaccines yielded sera which possessed markedly elevated γ-globulin. The sera of one rabbit immunized with Group A-variant vaccine possessed 55 mg/ml of γ-globulin. The bulk of this γ-globulin, identified as γG-globulin, was homogeneous by zone electrophoresis and of specificity directed against the Group A-variant carbohydrate antigen. L chains isolated from specific antibody obtained from an immune precipitate were distributed as a single band on starch gel electrophoresis, whereas the normal γ-globulin traveled as a diffuse smear. These data suggest that the rabbit streptococcal Group A-variant antibodies possess a limited range of physicochemical properties and electrophoretic mobility compared to that generally observed for the normal complement of γ-globulin.

Existence in Salmonid Hemoglobins of Molecular Species with Three and Four Different Polypeptides

1970 ◽  
Vol 27 (7) ◽  
pp. 1325-1328 ◽  
Author(s):  
H. Tsuyuki ◽  
A. P. Ronald
Keyword(s):  
Amino Acids ◽  
Molecular Species ◽  
Gel Electrophoresis ◽  
Sockeye Salmon ◽  
Pacific Salmon ◽  
Starch Gel Electrophoresis ◽  
Large Numbers ◽  
Starch Gel ◽  
Tetraploid Origin

The approximate equivalence of tryptic fragments and total basic amino acids per molecule of hemoglobin in five species of Pacific salmon, and the demonstration in sockeye salmon (Oncorhynchus nerka) of three or four electrophoretically distinct polypeptides in each of six major hemoglobin fractions separated by starch-gel electrophoresis, provided strong evidence for the in vivo existence in salmonids of molecular species of hemoglobins consisting of three and four different polypeptides. At least eight electrophoretically distinct polypeptides, including forms allelic to both the α- and β-type proteins, were found, accounting for the presence of large numbers of molecular species of hemoglobins and providing further evidence for the tetraploid origin of most salmonids.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

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