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.

CHANGES IN THE MULTIPLE HEMOGLOBIN PATTERNS OF SOME PACIFIC SALMON, GENUS ONCORHYNCHUS, DURING THE PARR–SMOLT TRANSFORMATION

1964 ◽  
Vol 42 (6) ◽  
pp. 697-703 ◽  
Author(s):  
W. E. Vanstone ◽  
Eve Roberts ◽  
H. Tsuyuki
Keyword(s):  
Life Cycle ◽  
Gel Electrophoresis ◽  
Sockeye Salmon ◽  
Coho Salmon ◽  
Pacific Salmon ◽  
Starch Gel Electrophoresis ◽  
Mature Adults ◽  
Salmon Fry ◽  
Starch Gel ◽  
Sexually Mature

By employing starch gel electrophoresis it has been found that coho salmon fry and smolts contain 10 anodal-migrating, and 12 cathodal-migrating, hemoglobin fractions. Prepuberal [Formula: see text]-year-old coho salmon caught at sea and sexually mature adults taken from fresh water contained the same anodal fractions and at approximately the same concentrations as were found in fry and smolts. However, the concentrations of the cathodal fractions had increased so that these were very nearly equal to those of the anodal fractions. Similar hemoglobin changes were found in both anadromous and land-locked sockeye salmon, but in this species seven anodal and six cathodal fractions were present at their "adult" concentrations in fry and smolts. Six other cathodal fractions which were absent entirely or present only in trace amounts in fry and smolts increased to their adult concentrations some time later in the life cycle of both varieties of sockeye. It is postulated that these changes reflect an ecological adaption to life in the ocean.

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.

Enzymatic Modifications of the Protamines. II. Separation and Characterization of Phosphorylated Species of Protamines from Trout Testis

1974 ◽  
Vol 52 (6) ◽  
pp. 536-546 ◽  
Author(s):  
Andrew J. Louie ◽  
Gordon H. Dixon
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Stage Of Development ◽  
Phosphorylated Amino Acid ◽  
Similar Series ◽  
Starch Gel ◽  
Derivatives Of

Substantial quantities of highly phosphorylated protamines were prepared from hormonally induced trout testes at the early protamine stage of development. Purified protamines from testes induced to mature by injection of salmon pituitary extracts were resolved into eight fractions on long carboxymethyl cellulose columns by eluting with a gradient of LiCl in the presence of 6 M urea; only two major fractions were found in protamine extracted from naturally maturing testes. Each fraction was not homogenous but consisted of a mixture of several related protamines. Analysis of radioactivity in in vivo32P-labeled protamine indicated that six of the eight fractions were phosphorylated. Amino acid analysis, phosphate determinations, and starch gel electrophoresis indicated that three of the phosphorylated peaks correspond to the mono-, di-, and triphosphorylated derivatives of the first fraction (three serines) of protamine, while the other three correspond to a similar series of the second fraction (four serines) of protamine. These protamines with differing levels of phosphorylation may be useful for in vitro studies of the interaction of phosphoprotamines with DNA or chromatin.

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.

A Study of Detergent Pollution By Molecular Methods: Starch Gel Electrophoresis of a Variety of Enzymes and Other Proteins

1967 ◽  
Vol 47 (3) ◽  
pp. 659-675 ◽  
Author(s):  
Clyde Manwell ◽  
C. M. Ann Baker
Keyword(s):  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Marine Species ◽  
Serum Lipoprotein ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Irreversible Effect ◽  
General Opinion

Tissues from a number of marine species were treated with a variety of solutions, including 1% of the major ‘detergent’ (B.P. 1002) used in attempting to disperse the oil from the ‘Torrey Canyon’ and 1% of each of the three major constituents of B.P. 1002, two of which are non-ionic surfactants.The extracts were submitted to vertical starch-gel electrophoresis in order to measure both the effect of the detergent in facilitating the breakdown of cellular structure (extractability), and the irreversible effect on activation or inhibition of various enzymes and other proteins.The proteins studied include a variety of NAD- and NADP-linked dehydrogenases, esterases, blood and nerve haemoglobins, plasma proteins, egg white and yolk proteins, and r-phycoerythrin.The results confirm the general opinion that detergents increase the extractability of proteins from cells. In particular lipoprotein systems are altered, e.g. ‘fast’ serum lipoprotein in fishes (and other vertebrates). Other effects are also observed, e.g. sole but not turbot haemoglobin is rendered relatively insoluble, probably because the detergent stabilizes haemoglobin binding to other components in the erythrocyte. Certain enzymes, e.g. some esterases and amylases, are activated—a not surprising observation. However, a few enzymes are altered in electrophoretic mobility or in activity in a way that one might not expect, e.g. bass Morone labrax lactate dehydrogenase.The results indicate that ‘oil-spill’ detergents and their constituent surfactants are biochemically quite powerful agents. It is too early to attempt to correlate in vitro and in vivo observations but there is an indication that starch-gel electrophoresis provides a useful supplement to more conventional methods used in the studies on complex pollution problems.

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.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

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