Timing of Changes in the Blood, Morphology, and Behavior of Petromyzon marinus During Metamorphosis

1972 ◽  
Vol 29 (9) ◽  
pp. 1277-1282 ◽  
Author(s):  
F. W. H. Beamish ◽  
I. C. Potter
Keyword(s):  
Short Duration ◽  
Gel Electrophoresis ◽  
Developmental Stages ◽  
Polyacrylamide Gel Electrophoresis ◽  
Petromyzon Marinus ◽  
Polyacrylamide Gel ◽  
Catostomus Commersoni ◽  
Blood Morphology ◽  
And Behavior ◽  
Behavioral Criteria

Morphological, biochemical, and behavioral criteria, from samples collected from 1969 to 1971, showed that metamorphosis in P. marinus is of a relatively short duration. In an analysis of sequential catches during 1971, the first external signs of transformation were observed only in samples caught between July 12 and 26, illustrating the marked synchrony characteristic of this and subsequent developmental stages. Relative increases in size of the disc and snout were most marked from mid-August to late October. Polyacrylamide gel electrophoresis showed that the change-over from larval to adult hemoglobins took place mainly between early August and late October, the beginning and peak of this process being characterised by reduced hematocrit values. Over 95% of the animals captured at various times in the field commenced feeding on suckers (Catostomus commersoni) in the laboratory by late November or early December.

Yolk proteins in salmon (Salmo salar) oocytes, eyed eggs, and alevins differing in viability

1990 ◽  
Vol 68 (5) ◽  
pp. 895-900 ◽  
Author(s):  
Thomas Olin ◽  
Alexandra von der Decken
Keyword(s):  
Molecular Weight ◽  
Salmo Salar ◽  
Gel Electrophoresis ◽  
Developmental Stages ◽  
Polyacrylamide Gel Electrophoresis ◽  
Specific Antigen ◽  
Protein Composition ◽  
Polyacrylamide Gel ◽  
Parental Origin ◽  
Yolk Proteins

The developmental stages of oocytes, eyed eggs, and alevins from salmon (Salmo salar) were compared for their yolk protein composition. In oocytes, SDS–polyacrylamide gel electrophoresis showed high amounts of a protein with the molecular weight (Mr) of 94 000. In eyed eggs, the 94 000 protein decreased and was undetectable in the alevins. Furthermore, in eyed eggs the proteins of 67 000, 30 000, and 27 000 increased, while in the alevins the concentration of the 67 000 protein decreased and that of the 39 000 increased. Vitellogenin-specific antigen sites analyzed by immunoblotting were most pronounced with the proteins of 94 000, 67 000, 39 000, 30 000, 23 000, and 19 000. Separation of the yolk proteins by HPLC gave four peaks at 280 nm for all three developmental stages. Each peak consisted of several proteins as analyzed by SDS–polyacrylamide gel electrophoresis. The 7-day-old alevins sampled from groups of different parental origin showed differences in the amount of the 67 000 and 23 000 proteins. Expectancy of survival within the group in connection with a slow disappearance of the 67 000 and 23 000 proteins was statistically significant. A fast disappearance may be used as an indication of, but not as the reason for, a high mortality within one group of alevins.

scholarly journals Biology of amazonian mosquitoes. III. Esterase isozymes in Anopheles darlingi.

1985 ◽  
Vol 15 (1-2) ◽  
pp. 167-178 ◽  
Author(s):  
Joselita M.M. dos Santos ◽  
Eucleia P.B. Contel ◽  
Warwick E. Kerr
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Developmental Stages ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Anopheles Darlingi ◽  
Genetic Studies ◽  
Esterase Isozymes ◽  
Phenotypic Distribution ◽  
Polymorphic System

Six esterase isozymes were studied during the development of Anopheles darlingi by using polyacrylamide gel electrophoresis and two different substrates, a-naphthylcelate and a-naphthylpropionate. Esterases 5 and 6'were detected in all developmental stages esterases 1 and 2 were more intensively stained if larvae, while esterases 3 and 4 were better visualized in pupae and adults. Strong differences in intensity of some of the isozymes were observed during the pupal stage.Four out of the six isozymes showed variation in the electrophoretic mobility. Esterase-2 was choosed for genetic studies, because was the best stained isozyme in the gels. Two codominant alleles {Est2*S and Est2*F) code for this polymorphic system, with the Est*S frequency equal to 0.521. Phenotypic distribution is in agreement with hardy-Weinberg expectations.

scholarly journals Genetic Polymorphism Based on β-napthyl Acetate in Different Age Group of Gambusia Affinis in Bangladesh

2012 ◽  
Vol 36 (1) ◽  
pp. 39-44
Author(s):  
Md Monjurul Ahasan ◽  
Md Anisur Rahman ◽  
AFM Jamal Uddin
Keyword(s):  
Genetic Polymorphism ◽  
Gel Electrophoresis ◽  
Developmental Stages ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gambusia Affinis ◽  
Polyacrylamide Gel ◽  
Age Group ◽  
Male And Female ◽  
Esterase Isozymes ◽  
Academy Of Sciences

Genetic polymorphism of esterase isozymes was examined in different developmental stages of Gambusia affinis after staining with ?-napthyl acetate as substrate by 7.5% polyacrylamide gel electrophoresis. Samples were just after birth, seven, 14 days old fry, 21, 28, 35, 42, 49 days old  male and female. Altogether three esterase bands named as Est-1, Est-2 and Est-3 were observed. Est-1 was absent in seven samples out of 13, Est-2 was absent only in just after birth, Est-3 was  absent in seven different samples out of 13 samples. This result indicates that Est-1 and Est-3 were  less active and Est-2 was very active at ? napthyl acetate. DOI: http://dx.doi.org/10.3329/jbas.v36i1.10917 Journal of Bangladesh Academy of Sciences, Vol. 36, No. 1, 39-44, 2012

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Platelet Microtubule Subunit Proteins

1979 ◽  
Vol 42 (05) ◽  
pp. 1630-1633 ◽  
Author(s):  
A G Castle ◽  
N Crawford
Keyword(s):  
Epithelial Cells ◽  
Gel Electrophoresis ◽  
Blood Platelets ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Lens Epithelial Cells ◽  
Molecular Weights ◽  
Kinetics Of ◽  
Microtubular Structures

SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS-polyacrylamide gel electrophoresis. These subunits associate as dimers with sedimentation coefficients of about 5.7 S although it is not known whether the dimer protein is a homo- or hetero-dimer. The dimer tubulin binds the anti-mitotic drug colchicine and the kinetics of this binding are similar to those reported for neurotubulins. Platelet microtubules also contain two HMW proteins which appear to be essential and integral components of the fully assembled microtubule. These proteins have molecular weights greater than 200,000 daltons. Fluorescent labelled antibodies to platelet and brain tubulins stain long filamentous microtubular structures in bovine lens epithelial cells and this pattern of staining is prevented by exposing the cells to conditions known to cause depolymerisation of cell microtubules.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

1979 ◽  
Author(s):  
C Cierniewski ◽  
T Krajewski ◽  
E Janiak
Keyword(s):  
Gel Electrophoresis ◽  
Functional Relationship ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Functional Similarity ◽  
Fractionation Method ◽  
Relationship Of ◽  
Fibrin Monomers ◽  
Fibrinogen Molecule ◽  
Cold Ethanol Fractionation

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

Identifikasi Daging Tikus Pada Produk Baso Dengan Metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE)

2018 ◽  
Vol 26 (2) ◽  
pp. 058
Author(s):  
Anna P. Roswiem ◽  
Triayu Septiani
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Sds Page

<em>Bahan<strong> </strong>baku untuk membuat baso adalah daging hewan, pada umumnya dari daging sapi, ayam, ikan dan babi. Di beberapa daerah di Indonesia terjadi kasus baso tikus. Tujuan penelitian ini adalah menguji ada tidaknya kandungan daging tikus pada produk baso yang dijual di pasar Cempaka Putih-Kecamatan Kramat Jakarta Pusat dan di pedagang baso atau mie baso di sekitar kampus Universitas YARSI Jakarta. Daging adalah protein salah satu metode untuk mengidentifikasi protein adalah metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE).<strong> </strong>Hasil penelitian menunjukkan bahwa dari 6 sampel baso terindikasi ada 2 sampel baso dengan nomor 1 dan 5 yang dibuat dari campuran daging sapi dan tikus; ada 1 sampel baso dengan nomor 6 yang terbuat dari daging tikus; dan 2 sampel baso dengan nomor 2 dan 3 yang terbuat dari campuran sapi  dan babi, dan hanya 1 sampel baso dengan nomor sampel 4 yang benar-benar terbuat dari daging sapi.</em>

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