Action of Factor XIII on Transamidation Bounds between the Collagen Molecule Constituents

1975 ◽  
Author(s):  
J. Soria ◽  
G. Soria ◽  
G. Boulard
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Factor Xiii ◽  
Phase Contrast ◽  
Polyacrylamide Gel Electrophoresis ◽  
The Other ◽  
Polymerization Process ◽  
Collagen Molecule ◽  
Phase Contrast Microscopy ◽  
Contrast Microscopy

By polyacrylamide gel electrophoresis in the presence of SDS we observed that collagen polymerized in the presence of factor XIII a, is dissociated by urea into sub-units with a higher molecular weight than that polymerized in the absence of factor XIII.In the other hand, by phase contrast microscopy we have found that the structure of collagen is quite different when the polymerization process takes place in the presence or in the absence of activated factor XIII.This modification of collagen polymerization in the presence of factor XIII a possibly acts in wound healing.

Isolation of Two Bovine Amelogenin Peptides and Their Amino Acid Sequences

1987 ◽  
Vol 1 (2) ◽  
pp. 276-281 ◽  
Author(s):  
J.-H. Yeh ◽  
T. Takagi ◽  
S. Sasaki
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Edman Degradation ◽  
Amino Acid Residues ◽  
Peptide Fractions

Two peptide fractions of bovine amelogenin having a highly aggregative property to form polymers were purified by chromatography, SDS-polyacrylamide gel electrophoresis, and HPLC. Amino acid sequences of purified peptides were determined by automated Edman degradation. One peptide was found to be composed of 63 amino acid residues having a molecular weight of 7105, and the other of 86 residues having that of 9683. The sequence of the smaller peptide was identical to the C-terminal 63 residues of the amelogenin molecule of 170 residues previously reported, but the larger contained eight residues which are absent in the amelogenin sequence. There is a possibility that the latter peptide might be synthesized independently from mRNA spliced at different positions.

Compound sensilla in monogenean skin parasites

Parasitology ◽  
1969 ◽  
Vol 59 (3) ◽  
pp. 625-636 ◽  
Author(s):  
Kathleen M. Lyons
Keyword(s):  
Fine Structure ◽  
Electron Microscope ◽  
Phase Contrast ◽  
The Other ◽  
Phase Contrast Microscopy ◽  
Sense Organs ◽  
Dense Membrane ◽  
Contrast Microscopy ◽  
Membrane Bound

The fine structure of two kinds of compound presumed sense organs from the heads of three skin parasitic monogeneans Gyrodactylus sp. Entobdella soleae (larva only) and Acanthocotyle elegans is described. One kind of compound receptor consists of a number of associated sensilla, each ending in a single cilium (the spike sensilla of Gyrodactylus and the cone sensilla of E. soleae oncomiracidium).The other kind of compound organ is made up of one or a few neurones only, each of which bears many cilia (pit organs of E. soleae oncomiracidium and feeding organ sensilla of Acanthocotyle elegans). The spike sensilla of Gyrodactylus have also been studied using a Cambridge Instrument Co. Stereoscan electron microscope and by phase-contrast microscopy. The ciliary endings of all these sense organs are highly modified and have lost the 9 + 2 structure, being packed with many fibres. The fibre arrangement in the cilia of the cone sensillae of E. soleae oncomiracidium and the feeding organ sensilla of A. elegans has been compared with that in the ciliary endings of other invertebrate mechano- and chemoreceptors. The possibility that the spike sensilla of Gyrodactylus may be chemoreceptors has been discussed but it is considered premature to attempt to assign functions to the other sense organs studied. Electron dense membrane-bound inclusions occurring specifically in the nerves supplying the spike sensilla of Gyrodactylus may be neurosecretory.

scholarly journals New Exfoliative Toxin Produced by a Plasmid-Carrying Strain of Staphylococcus hyicus

1999 ◽  
Vol 67 (8) ◽  
pp. 4014-4018 ◽  
Author(s):  
Hisaaki Sato ◽  
Takao Watanabe ◽  
Yasuko Murata ◽  
Ayumi Ohtake ◽  
Mayumi Nakamura ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Staphylococcus Aureus ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
The Other ◽  
Exfoliative Toxin ◽  
Sds Page ◽  
Serotype B

ABSTRACT A new serotype of Staphylococcus hyicus exfoliative toxin (SHET), serotype B, was isolated from the culture filtrate of a plasmid-carrying strain of S. hyicus. The new SHET was purified by precipitation with 70% saturated ammonium sulfate, gel filtration on a Sephadex G-75 column, column chromatography on DEAE–Cellulofine A-500, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The new SHET caused exfoliation of the epidermis as determined by the so-called Nikolsky sign when inoculated into 1-day-old chickens. The new SHET was serologically different fromStaphylococcus aureus exfoliative toxins (ETs) (ETA, ETB, and ETC) and from the SHET from the plasmidless strain but showed the same molecular weight as the other serotypes of toxins on SDS-PAGE. It was thermolabile and lost its toxicity after being heated at 60°C for 30 min. We propose that the new SHET be designated SHETB and that the SHET produced by the plasmidless strain be designated SHETA.

INFLUENCE OF SOURCE OF WHEAT CYTOPLASM ON THE NATURE OF PROTEINS IN HEXAPLOID TRITICALE

1974 ◽  
Vol 16 (3) ◽  
pp. 529-537 ◽  
Author(s):  
S. L. K. Hsam ◽  
E. N. Larter
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Triticum Aestivum L ◽  
The Other ◽  
Hexaploid Triticale ◽  
Electrophoretic Patterns ◽  
High Molecular Weight Proteins

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to study seed proteins in 4 pairs of reciprocal F1 isogenic hybrids of hexaploid triticales differing only in their source of cytoplasm. One member of each reciprocal pair possessed the cytoplasm of hexaploid (6x) wheat (Triticum aestivum L. em. Thell), the other, the cytoplasm from tetraploid (4x) wheat (T. turgidum L). Qualitative as well as quantitative differences were observed in the electrophoretic patterns of the albumins and globulins. High molecular weight proteins (> 34,000 daltons) were synthesized in triticale with 6x wheat cytoplasm in greater quantity than in triticale with 4x wheat cytoplasm. Differences in the patterns of gliadin and reduced glutenin of the reciprocal triticale populations were quantitative. The relevance of these findings to seed development in triticales is discussed.

Soluble High-Molecular-Weight E Fragments in the Plasmin-Induced Degradation Products of Cross-Linked Human Fibrin

1975 ◽  
Vol 49 (2) ◽  
pp. 149-156 ◽  
Author(s):  
P. J. Gaffney ◽  
D. A. Lane ◽  
M. Brasher
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gel Electrophoresis ◽  
Factor Xiii ◽  
Degradation Products ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cross Linking ◽  
D Dimer

1. The factor XIII-mediated cross-linked α chains in fibrin have no effect on the nature of the fragments released during the solubilization of fibrin by plasmin. 2. Besides the known D dimer and E fragments solubilized during the lysis of cross-linked fibrin, other fragments have been observed on sodium dodecyl sulphate-polyacrylamide gel electrophoresis which have a molecular weight of about 135 000. After prolonged plasmin digestion, these fragments (U fragments) were no longer evident on the gels and the high-molecular-weight E antigen was absent. It is assumed that the E antigen was associated with the U fragments. These fragments also cross-reacted with an anti-D serum. 3. The U fragments have been tentatively presumed to be a factor XIII-mediated cross-linked D–E complex since they degrade only after prolonged degradation with plasmin. Whereas it is known that the fibrin D dimer fragment contains the cross-linked γ chain residues of the originating fibrin, the presumed covalent cross-linking of the D–E fragments has not been proved. 4. The presence of these high-molecular-weight fragments, containing the E antigen, in cross-linked human fibrin digests should be taken into account in the development of D dimer assays to monitor fibrin lysis in vivo.

Counting dead spermatozoa in frozen semen

1965 ◽  
Vol 7 (1) ◽  
pp. 59-65 ◽  
Author(s):  
H. R. L. Buttle ◽  
J. L. Hancock ◽  
A. F. Purser
Keyword(s):  
Analysis Of Variance ◽  
Sodium Fluoride ◽  
Phase Contrast ◽  
Egg Yolk ◽  
The Other ◽  
Phase Method ◽  
Phase Contrast Microscopy ◽  
Frozen Semen ◽  
Contrast Microscopy ◽  
Differential Counts

SUMMARYThree methods were used to make differential counts of living and dead bull spermatozoa in samples of frozen semen in an egg-yolk citrate medium containing glycerol.With two methods (‘phase’ and ‘nigrosin’ methods) dead spermatozoa were identified by their altered structure. With a third method (nigrosineosin) dead spermatozoa were identified by their staining affinity. With the phase method spermatozoa were immobilised by treatment with approximately M/40 sodium fluoride and were examined by phase-contrast microscopy in unfixed wet preparations. With the other two methods the spermatozoa were examined in smears stained either with nigrosin alone (nigrosin method) or with nigrosin and eosin (nigrosin-eosin method).Analysis of variance of the results of a factorial experiment involving fluoride-treated and untreated samples from 6 bulls with the three methods showed that differences between semen samples contributed 66% of the variation. A defect of the phase method was that the variance between counts was greater than the theoretically expected value.All spermatozoa in nigrosin-eosin stained preparations were stained with eosin within a few days of the smears being made, so that living and dead spermatozoa could not be distinguished by their differing affinities for eosin. Repeat counts on nigrosin-stained preparations did not differ significantly from counts made several days previously. Sodium fluoride in the concentration used here (M/40) tended to reduce the percentage of dead spermatozoa.

Reversible inhibition of chondrogenic expression by certain hyaluronidase preparations

Development ◽  
1979 ◽  
Vol 53 (1) ◽  
pp. 91-102
Author(s):  
John P. Pennypacker ◽  
Paul F. Goetinck
Keyword(s):  
Growth Rate ◽  
Phase Contrast ◽  
The Other ◽  
Phase Contrast Microscopy ◽  
Embryonic Chick ◽  
Minimum Concentration ◽  
Contrast Microscopy ◽  
Matrix Accumulation ◽  
Testicular Hyaluronidase

Embryonic chick chondrocytes were cultured in the presence or absence of different preparations of testicular hyaluronidase. This treatment inhibited the accumulation of cartilage matrix as indicated by phase-contrast microscopy, by Alcian green staining, and by accumulation of 35S-labeled material. In addition, most preparations of testicular hyaluronidase caused a conversion of the cells to a fibroblastic phenotype characterized by a faster growth rate and the synthesis of type-1 collagen. This effect was found to beconcentrationdependent and was not observed at the minimum concentration of hyaluronidase required toinhibit matrix accumulation. Since two more highly purified hyaluronidase preparations prevented matrix accumulation but did not cause the fibroblastic transformation, it is likely that the conversion to a fibroblastic phenotype is caused by a contaminant in the other hyaluronidase preparations.

Human beta-globulin factors affecting growth of human lymphocytes and mouse fibroblasts

1980 ◽  
Vol 44 (1) ◽  
pp. 285-297
Author(s):  
H. Thomou ◽  
S. Koussoulakos ◽  
D. Stathakos
Keyword(s):  
Molecular Weight ◽  
Biological Activity ◽  
Gel Electrophoresis ◽  
Human Lymphocytes ◽  
Polyacrylamide Gel Electrophoresis ◽  
The Other ◽  
Factors Affecting ◽  
Mouse Fibroblasts ◽  
Beta Globulin ◽  
Growth Promoting

Evidence is presented to show the existence in human beta-globulin (Cohn fraction III) of 2 growth-promoting factors that stimulate DNA synthesis and cell division in human lymphocytes and 3T3 B mouse fibroblasts. After extraction of human beta-globulins at pH 3.0 in 0.1 M NaCl followed by sieve chromatography on Sephadex, 2 distinct fractions were obtained containing the biological activity; one of polypeptide nature and molecular weight of approx. 10 000 Daltons and the other consisting of a homogeneous ribonucleic acid, as revealed by polyacrylamide gel electrophoresis. The above-mentioned factors appear to lack both cell and species specificity, since they are mitogenic agents for cells as diverse as mouse fibroblasts and human lymphocytes.

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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.

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