scholarly journals Esterase variability in different tissues of Naked Neck Fowl (Gallus gallus domesticus) of Bangladesh using polyacrylamide gel electrophoresis

1970 ◽  
Vol 8 (1) ◽  
pp. 51-55
Author(s):  
QS Akter ◽  
KA Muid ◽  
KMA Tareq ◽  
MAMY Khandoker
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gallus Gallus ◽  
Gallus Domesticus ◽  
Polyacrylamide Gel ◽  
Gallus Gallus Domesticus ◽  
Esterase Isozyme ◽  
Indigenous Chicken ◽  
Naked Neck ◽  
Different Tissues

Naked neck fowl (Gallus gallus domesticus) comprises one of the indigenous chicken populations in Bangladesh. The present investigation was conducted to study the polymorphic pattern of the estrase isozyme in different tissues of the fowl by polyacrylamide gel electrophoresis (PAGE) system. In this experiment, α-napthyle and β-napthyle acetate were used as substrate. Esterase variability of different samples of fore brain, mid brain, hind brain, heart brain, liver, testis, oesophagus, gizzard, bile ducts, proventiculus, small intestine, large intestine pectoral muscle, pelvic muscle, lung, eye, kidney, pancreas, body muscle and blood cells were examined. Altogether four esterase bands were observed and the bands were designated as Esterase Est-1 2.0, Est-21.0 Est-30.75 and Est-40.15. Among the four bands Est-1 was the fastest and placed near to anode (+) electrode. Esterase showed tissue specific variation. Est-2 was found in almost all tissues, whereas Est-1 was observed only in liver. Est-3 and Est-4 were expressed exclusively in the nervous system especially in brain. Such findings may provide basic information to analyze the esterase activity in different tissues. Keywords: Esterase; Isozyme; Naked neck fowl; Tissue DOI: 10.3329/jbau.v8i1.6398J. Bangladesh Agril. Univ. 8(1): 51-55, 2010

scholarly journals The small dermatan sulphate proteoglycans synthesized by fibroblasts derived from skin, synovium and gingiva show tissue-related heterogeneity

1988 ◽  
Vol 256 (1) ◽  
pp. 35-40 ◽  
Author(s):  
H Larjava ◽  
J Heino ◽  
T Krusius ◽  
E Vuorio ◽  
M Tammi
Keyword(s):  
Extracellular Matrix ◽  
Molecular Mass ◽  
Gel Electrophoresis ◽  
Core Protein ◽  
Culture Media ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Gingival Fibroblasts ◽  
Dermatan Sulphate ◽  
Different Tissues

Dermatan sulphate proteoglycans (DSPGs) synthesized in the presence of 35SO4 were characterized in culture media of fibroblast lines obtained from skin, synovium, and gingiva. The molecular mass of DSPG varied from 95-130 kDa as estimated by SDS/polyacrylamide-gel electrophoresis. Gingival fibroblasts constantly produced larger DSPGs than skin fibroblasts. This was due to the larger dermatan sulphate (DS) chains, which also showed tissue-related heterogeneity in the distribution of 4- and 6-sulphated disaccharide units. The N-glycosylated cores (44 and 47 kDa) obtained following chondroitinase ABC treatment were of identical size in all tissues. The cores from the different tissues were also of the same size (38 kDa) when addition of the N-linked oligosaccharides was inhibited by tunicamycin or when they were removed by N-glycanase treatment. No evidence for low-molecular-mass sulphated oligosaccharides was found. All tissues contained two mRNA species (1.6 and 1.9 kb) for the DSPG core protein. These data suggest that the pattern of transferase activities involved in the construction of DS chains differs from one tissue to another. This variation may modulate the functions of DSPG in the extracellular matrix.

scholarly journals Tissue Specific Esterase Expression In Indigenous Chicken Of Bangladesh

1970 ◽  
Vol 38 (1-2) ◽  
pp. 15-21
Author(s):  
RM Shahjahan ◽  
KA Muid ◽  
QS Akter ◽  
KMA Tareq ◽  
RA Begum ◽  
...  
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Relative Mobility ◽  
Indigenous Chicken ◽  
Naked Neck ◽  
Genetic Groups ◽  
Red Jungle Fowl ◽  
Close Relationship ◽  
Esterase Gene ◽  
Almost All

The present investigation was done in the esterase gene expression analysis of the Red Jungle fowl Gallus gallus of Bangladesh utilizing the polyacrylamide gel electrophoresis (PAGE) technique. Each allele produces a biochemical message that helps to produce various protein phenotypes those were expressed in the form of bands on the polyacrylamide gel bed. Altogether four different esterase bands were recorded in both Red Jungle (RJ) fowl and Naked Neck (NN) fowl of Bangladesh. These were denoted as Est-1 (2), Est-2(1), Est-3 (21) and Est-4 (13) based on the relative mobility on the gel. Among them Est-2 is very common in almost all tissues. Comparing the esterase in both genetic groups, their expression intensity even the relative mobility provided a unique feature that they were similar. The investigation indicates that esterase gene between the Red Jungle fowl and Naked Neck fowl of Bangladesh has a close relationship. DOI: http://dx.doi.org/10.3329/bjas.v38i1-2.9908 BJAS 2009; 38(1-2): 15-21

scholarly journals Short Communication: The type and sound diversity of Kukuak Balenggek chicken (Gallus gallus domesticus) reared in West Sumatra, Indonesia

2020 ◽  
Vol 21 (5) ◽  
Author(s):  
Firda Arlina ◽  
RUSFIDRA ◽  
DICKY ANDRIANO ◽  
CECE SUMATRI
Keyword(s):  
Short Communication ◽  
Computer Software ◽  
Gallus Gallus ◽  
Gallus Domesticus ◽  
Survey Method ◽  
Gallus Gallus Domesticus ◽  
Adult Males ◽  
Indigenous Chicken ◽  
West Sumatra

Abstract. Arlina F, Rusfidra, Andriano D, Sumatri C. 2020. Short Communication: The type and sound diversity of Kukuak Balenggek chicken (Gallus gallus domesticus) reared by the association of Kukuak Balenggek Chicken Lovers in West Sumatra. Biodiversitas 21: 1914-1919. Kukuak Balenggek is one of the rare indigenous chicken in Indonesia. The number of population and genetic quality of Kukuak Balenggek Chicken (KBC) in in-situ has been decreasing from year to year. This encourages Kukuak Balenggek chicken lovers to found an association, namely Kukuak Balenggek Chicken Lovers, in order to conserve the germplasm native to West Sumatra. This study aimed to identify the type dan the song diversity of Kukuak Balenggek Chicken. A total of 180 adult males of Kukuak Balenggek chicken used in this study came from 32 members of the Association of Kukuak Balenggek Chicken Lovers. The survey method used in this research was purposive sampling. The analysis of data was carried out by descriptive statistical analysis. The parameters observed were the type of sound, number of crowing, number of crowing syllables, and duration of crow. The analysis of Kukuak Balenggek sound used the Cool Record Edit Pro computer software. The result showed that the percentage of sound type of Rantak Gumarang, Sigegek Angin, Alang Babega, Riak Ilia Aia, Ginyang, Ginyang Mataci, Gayuang Luluah were 37.78%, 26.67 %, 7.78%, 13.33%, 3.33%, 5.56%, and 5,56%, respectively. The highest of average, the number of crowing and syllable crowing based on the type of KBC sound was Sigegek Angin sound with an average of 9.48 crowing and 12.48 crowing syllable. While the longest average of Kukuak Balenggek chicken crowing duration was the Gayuang Luluah sound type with an average of 3.33 seconds.

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.

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