Identification of gene products expressed in the developing chick visual system: characterization of a middle-molecular-weight neurofilament cDNA.

Three c-yes cDNA clones were obtained from poly(A)+ RNA of human embryo fibroblasts. Sequence analysis of the clones showed that they contained inserts corresponding to nearly full-length human c-yes mRNA, which could encode a polypeptide of 543 amino acids with a relative molecular weight (Mr) of 60,801. The predicted amino acid sequence of the protein has no apparent membrane-spanning region or suspected ligand binding domain and closely resembles pp60c-src. Comparison of the sequences of c-yes and v-yes revealed that the v-yes gene contains most of the c-yes coding sequence except the region encoding its extreme carboxyl terminus. The region missing from the v-yes protein is the part that is highly conserved in cellular gene products of the protein-tyrosine kinase family.

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Characterization of cDNA clones for the human c-yes gene.

Molecular and Cellular Biology ◽

10.1128/mcb.7.1.41 ◽

1987 ◽

Vol 7 (1) ◽

pp. 41-47 ◽

Cited By ~ 73

Author(s):

J Sukegawa ◽

K Semba ◽

Y Yamanashi ◽

M Nishizawa ◽

N Miyajima ◽

...

Keyword(s):

Molecular Weight ◽

Protein Tyrosine Kinase ◽

Carboxyl Terminus ◽

Predicted Amino Acid Sequence ◽

Cdna Clones ◽

Gene Products ◽

Cellular Gene ◽

Relative Molecular Weight ◽

Membrane Spanning

Three c-yes cDNA clones were obtained from poly(A)+ RNA of human embryo fibroblasts. Sequence analysis of the clones showed that they contained inserts corresponding to nearly full-length human c-yes mRNA, which could encode a polypeptide of 543 amino acids with a relative molecular weight (Mr) of 60,801. The predicted amino acid sequence of the protein has no apparent membrane-spanning region or suspected ligand binding domain and closely resembles pp60c-src. Comparison of the sequences of c-yes and v-yes revealed that the v-yes gene contains most of the c-yes coding sequence except the region encoding its extreme carboxyl terminus. The region missing from the v-yes protein is the part that is highly conserved in cellular gene products of the protein-tyrosine kinase family.

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Isolation and Characterization of Plasminogen Activator from Pig Leucocytes

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649147 ◽

1974 ◽

Vol 31 (01) ◽

pp. 072-085 ◽

Cited By ~ 5

Author(s):

M Kopitar ◽

M Stegnar ◽

B Accetto ◽

D Lebez

Keyword(s):

Molecular Weight ◽

Plasminogen Activator ◽

Gel Electrophoresis ◽

Gel Filtration ◽

Ph Optimum ◽

Isolation And Characterization ◽

Ph Range ◽

Inhibition Studies ◽

Final Purification

SummaryPlasminogen activator was isolated from disrupted pig leucocytes by the aid of DEAE chromatography, gel filtration on Sephadex G-100 and final purification on CM cellulose, or by preparative gel electrophoresis.Isolated plasminogen activator corresponds No. 3 band of the starting sample of leucocyte cells (that is composed from 10 gel electrophoretic bands).pH optimum was found to be in pH range 8.0–8.5 and the highest pH stability is between pH range 5.0–8.0.Inhibition studies of isolated plasminogen activator were performed with EACA, AMCHA, PAMBA and Trasylol, using Anson and Astrup method. By Astrup method 100% inhibition was found with EACA and Trasylol and 30% with AMCHA. PAMBA gave 60% inhibition already at concentration 10–3 M/ml. Molecular weight of plasminogen activator was determined by gel filtration on Sephadex G-100. The value obtained from 4 different samples was found to be 28000–30500.

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Studies on the Characterization of Factor VIII and a Co-factor VIII

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649167 ◽

1974 ◽

Vol 31 (02) ◽

pp. 328-338

Author(s):

M. M. P Paulssen ◽

H. L. M. A Vandenbussche-Scheffers ◽

P. B Spaan ◽

T de Jong ◽

M. C Planje

Keyword(s):

Molecular Weight ◽

Factor Viii ◽

The Body ◽

Haemophilia A ◽

Von Willebrand's Disease ◽

Von Willebrand’S Disease ◽

Polysaccharide Content ◽

Plasma Factor ◽

Two Factors

SummaryFactor VIII occurs in the body in two different forms. In lymph factor VIII is bound to chylomicra. In plasma, factor VIII is bound to a protein.After delipidation of chylomicra we obtained a glycoprotein with a high polysaccharide content and a molecular weight of approx. 160,000.In plasma, factor VIII is attached to a protein which is present in normal concentrations in plasma of patients with haemophilia A and in serum (co-factor VIII).This factor is deficient in both the plasma and the serum of patients with von Willebrand’s disease.The binding between factor VIII and co-factor VIII is reversible.Some properties of these two factors are described.

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Rapid Isolation of High Molecular Weight Urokinase from Native Human Urine

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657167 ◽

1982 ◽

Vol 47 (03) ◽

pp. 197-202 ◽

Cited By ~ 23

Author(s):

Kurt Huber ◽

Johannes Kirchheimer ◽

Bernd R Binder

Keyword(s):

Molecular Weight ◽

High Molecular Weight ◽

Human Urine ◽

Gel Filtration ◽

Chain Structure ◽

The Other ◽

Single Chain ◽

Apparent Homogeneity ◽

Sequential Adsorption

SummaryUrokinase (UK) could be purified to apparent homogeneity starting from crude urine by sequential adsorption and elution of the enzyme to gelatine-Sepharose and agmatine-Sepharose followed by gel filtration on Sephadex G-150. The purified product exhibited characteristics of the high molecular weight urokinase (HMW-UK) but did contain two distinct entities, one of which exhibited a two chain structure as reported for the HMW-UK while the other one exhibited an apparent single chain structure. The purification described is rapid and simple and results in an enzyme with probably no major alterations. Yields are high enough to obtain purified enzymes for characterization of UK from individual donors.

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

10.1055/s-0038-1665670 ◽

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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