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.

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.

The Separation of Insect Haemolymph Proteins

1964 ◽  
Vol 96 (1-2) ◽  
pp. 110-110
Author(s):  
B. G. Loughton ◽  
P. Rueffel ◽  
H. Stich ◽  
A. S. West
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Homologous Proteins ◽  
Agar Gel ◽  
Diffusion Technique ◽  
Starch Gel ◽  
Rapid Characterization ◽  
Gel Diffusion

It has been suggested that information on the phylogenetic relationships of genera and species could be obtained by comparing the amino acid sequence in the homologous proteins of different species. This procedure is extremely difficult and time-consuming.However, a relatively rapid characterization of proteins can be obtained by analysing their mobilities with starch-gel electrophoresis and examination of antigenic diversity by the agar gel diffusion technique of Ouchterlony.

scholarly journals Electrophoretic Characterization of Taxus Cultivars

1993 ◽  
Vol 3 (4) ◽  
pp. 430-433
Author(s):  
C.E. Greer ◽  
R.E. Schutzki ◽  
A. Fernandez ◽  
J.F. Hancock
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel

Starch gel electrophoresis was used to fingerprint 55 Taxus plants, listed as 21 species and/or cultivars. Plants were analyzed for six enzymes, representing eight putative loci. Within many of the cultivars, different fingerprints were observed, indicating nomenclatural errors in Taxus.

scholarly journals Characterization of Enterobacteria by Starch-Gel Electrophoresis of Glucose-6-Phosphate Dehydrogenase and Phosphogluconate Dehydrogenase

1967 ◽  
Vol 94 (3) ◽  
pp. 544-551 ◽  
Author(s):  
James E. Bowman ◽  
Robert R. Brubaker ◽  
Henri Frischer ◽  
Paul E. Carson
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Phosphogluconate Dehydrogenase ◽  
Starch Gel ◽  
Glucose 6 Phosphate Dehydrogenase

In vivo effects of sodium fluoride on serum proteins and enzymes as studied with starch gel electrophoresis

1965 ◽  
Vol 10 (1) ◽  
pp. 107-IN24 ◽  
Author(s):  
E. Riekstniece ◽  
H.M. Myers ◽  
L.E. Glass
Keyword(s):  
Sodium Fluoride ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
In Vivo Effects

scholarly journals Isolation and Characterization of Protein Bodies From Developing Wheat Endosperm

1963 ◽  
Vol 16 (2) ◽  
pp. 375 ◽  
Author(s):  
Janet SD Graham ◽  
RK Morton ◽  
JK Raison
Keyword(s):  
Electron Microscopy ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Separation And Purification ◽  
Isolation And Characterization ◽  
Dense Bodies ◽  
Starch Gel ◽  
Slow Moving ◽  
Protein Components

Procedures are described for separation and purification of electron-dense bodies previously observed in intact endosperm by electron microscopy. Isolated bodies consist largely of protein. By starch-gel electrophoresis, the bodies contain predominantly slow-moving protein components similf1l' to those found in acetic acid extracts of whole endosperm.

scholarly journals The induction of cross-links in soluble rat skin collagen in vitro

1969 ◽  
Vol 114 (3) ◽  
pp. 509-512 ◽  
Author(s):  
D. W. Bannister
Keyword(s):  
Gel Electrophoresis ◽  
Subunit Composition ◽  
Starch Gel Electrophoresis ◽  
Rat Skin ◽  
Skin Collagen ◽  
Cross Linkage ◽  
Starch Gel ◽  
Cross Links

1. Starch-gel electrophoresis was used to investigate the subunit composition of salt-soluble and acid-soluble rat skin collagen. 2. Cross-linkage of collagen subunits in vitro was performed (a) when in fibrillar form and (b) when in solution. In the former case the increase in number of cross-links appeared to be predominantly intermolecular and in the latter case predominantly intramolecular.

scholarly journals Characterization of tissue alkaline phosphatases and their partial purification by starch-gel electrophoresis

1961 ◽  
Vol 81 (2) ◽  
pp. 441-447 ◽  
Author(s):  
DW MOSS ◽  
DM CAMPBELL ◽  
E ANAGNOSTOU-KAKARAS ◽  
EJ KING
Keyword(s):  
Gel Electrophoresis ◽  
Partial Purification ◽  
Starch Gel Electrophoresis ◽  
Alkaline Phosphatases ◽  
Starch Gel

scholarly journals Starch-gel Electrophoresis in the Characterization of Products of Collagen Breakdown.

1967 ◽  
Vol 21 ◽  
pp. 827-827 ◽  
Author(s):  
R. Penttinen ◽  
A. Kari ◽  
E. Kulonen ◽  
Åke Nilsson ◽  
H. Theorell ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel
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