PURIFICATION OF CA-7, A THROMBOLYTIC FUNGAL PROTEASE

1967 ◽  
Vol 45 (7) ◽  
pp. 1055-1065 ◽  
Author(s):  
D. A. J. Ives ◽  
A. L. Tosoni
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Total Absence ◽  
Acetone Treatment ◽  
Pure Amino Acid ◽  
Fungal Protease

Procedures are described for the purification of a thrombolytic fungal protease. These include precipitation with either lignin or tannin, removal of lignin or tannin with acetone, treatment with Benzathine, dialysis, passage through DEAE-Sephadex A-50 and Sephadex G-50, and finally lyophilization. The final product has a molecular weight of about 22,000 and is substantially pure. Amino acid analysis reveals a total absence of cysteine and cystine. The anomalous retention by Sephadex G-50 is discussed.

Acid Proteases From Species of Mucor: Molecular Weight of Mucor miehei Protease From Amino Acid Analysis Data

1973 ◽  
Vol 51 (12) ◽  
pp. 1638-1646 ◽  
Author(s):  
W. S. Rickert ◽  
J. R. Elliott
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Weight Function ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Amino Acid Analysis ◽  
Analysis Data ◽  
Improved Method ◽  
Mucor Miehei ◽  
A Value

An improved method for the isolation of Mucor miehei protease which utilizes a diafiltration cell has been used to obtain a highly purified protein in gram quantities and yields of about 80%. Based on a modified molecular weight function and data from amino acid analysis, a value of 41 800 for the molecular weight of the glycoprotein was established and some modification to the published amino acid composition was made. These results suggest that Mucor miehei protease is distinctly different from the two other acid proteases which are also produced by species of Mucor.

scholarly journals The isolation of three neurophysins from porcine posterior pituitary lobes

1970 ◽  
Vol 116 (5) ◽  
pp. 899-909 ◽  
Author(s):  
L. O. Uttenthal ◽  
D. B. Hope
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Gel Filtration ◽  
Biological Significance ◽  
Starch Gel Electrophoresis ◽  
Posterior Pituitary ◽  
Fresh Tissue ◽  
Molecular Weights ◽  
Molecular Dimensions

1. Three neurophysins, proteins that bind the polypeptide hormones oxytocin and vasopressin, have been isolated from acetone-dried porcine posterior pituitary lobes. The proteins have been named porcine neurophysins-I, -II and -III in order of their electrophoretic mobilities at pH8.1. 2. Electrophoretic comparison of the purified proteins, which are homogeneous on starch-gel electrophoresis, with the soluble proteins of fresh porcine posterior pituitary lobes extracted in 0.1m-HCl and in buffer pH8.1 suggests that the isolated proteins are native to the fresh tissue. 3. Neurophysins-I and -II are present in similar amounts in the tissue, whereas neurophysin-III is present only in small quantities. Acetone-dried tissue also contains traces of other hormone-binding neurophysin components. 4. All the neurophysins can bind both oxytocin and [8-lysine]-vasopressin. 5. The apparent molecular weights of the neurophysins increase with increasing protein concentration as measured by equilibrium sedimentation in the ultracentrifuge. 6. Neurophysins-I and -III are of similar molecular dimensions, contain one residue of methionine per molecule and lack histidine. The minimum molecular weight of neurophysin-I obtained by amino acid analysis is 9360. Neurophysin-II is of larger molecular dimensions than neurophysins-I and -III and can be separated from these by gel filtration on Sephadex G-75. It contains no histidine or methionine, and its minimum molecular weight has been estimated as 14020 by amino acid analysis. 7. Each of the three neurophysins possesses N-terminal alanine. 8. The possible biological significance of the existence of several neurophysins within one species is discussed.

scholarly journals Presence of histones in Aspergillus nidulans.

1976 ◽  
Vol 68 (3) ◽  
pp. 430-439 ◽  
Author(s):  
R A Felden ◽  
M M Sanders ◽  
N R Morris
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Amino Acid Analysis ◽  
Gel Chromatography ◽  
Mobility Patterns ◽  
Net Charge ◽  
Basic Proteins ◽  
Calf Thymus

Five major histone proteins have been extracted from chromatin isolated from purified nuclei of the fungus, Aspergillus nidulans. These proteins had chromatographic properties which were similar to reference calf thymus histones and were purified to electrophoretic homegeneity by gel chromatography of Bio-Gel P10, Bio-Gel P60, and Sephadex G-100. Electrophoresis of these proteins in three different systems (urea-starch, urea-acetic acid polyacrylamide, and discontinuous SDS polyacrylamide) showed that the A. nidulans histones H3 and H4 were nearly identical to calf thymus H3 and H4 with respect to net charge and molecular weight criteria, whereas the fungal histones H1, H2a and H2b were similar but not identical to the corresponding calf thymus histones. Amino acid analysis of A. nidulans histones H2a, H2b, and H4 showed them to be closely related to the homologous calf thymus histones. The mobility patterns of A. nidulans ribosomal basic proteins in three different electrophoretic systems were distinctly different from those of the fungal histones.

A Resolution of Reported Discrepancies in the Characteristics of Platelet Glycoproteins IV (GPIV) and III b (GPIII b)

1990 ◽  
Vol 63 (01) ◽  
pp. 097-102 ◽  
Author(s):  
Naomasa Yamamoto ◽  
Christophe de Romeuf ◽  
Narendra N Tandon ◽  
G A Jamieson
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Surface Glycoprotein ◽  
Differentiation Antigen ◽  
Platelet Surface ◽  
Crossed Immunoelectrophoresis ◽  
Methionine Residues

SummaryThe terms glycoprotein IV (GPIV) and glycoprotein IIIb (GPIIIb) have been used interchangeably and reports in the literature have indicated this glycoprotein as having a molecular weight variously described as either 88,000 or 97,000, a fast anodal mobility on crossed electrophoresis and either 13 or <1 methionine residues on amino acid analysis of the purified glycoprotein. To resolve these discrepancies, we have evaluated the characteristics of GPIV both in whole platelets and after isolation. These studies have shown that the term GPIV defines a protease-resistant platelet surface glycoprotein with Mr 88,330 ± 2,240 which is immunologically identical with the CD36 differentiation antigen, which migrates with a relatively slow anodal mobility on crossed immunoelectrophoresis and which contains ∼13 methionine residues per mole.

Human Prothrombin: A New Method of Preparation from a Single Individual

1973 ◽  
Vol 30 (03) ◽  
pp. 425-436 ◽  
Author(s):  
Richard Benarous ◽  
Dominique Labie ◽  
François Josso
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Good Yield ◽  
New Method ◽  
Single Individual ◽  
Single Chain ◽  
Simple Method ◽  
Terminal Residue ◽  
Sds Electrophoresis

SummaryA simple method for purification of human prothrombin from ACT) plasma of one single individual is described. This method is based on three steps :1. isolation of crude prothrombin complex by barium citrate adsorption;2. first purification by hydroxyapatite chromatography;3. further purification by DEAE Sephadex chromatography.The final product was obtained with a good yield and exhibited less than 5 p. cent contamination. The human purified prothrombin obtained in this way displays :– one single chain by SDS electrophoresis,– a molecular weight of 75,000-80,000 daltons,– a pi value pH 4.4 by electrofocusing,– Alanine as थ terminal residue.Amino-acid analysis is reported.

scholarly journals Colouring Matters of the Aphidoidea XLII. Purification and Properties of the Cyclising Enzyme [Protoaphin Dehydratase (Cyclising)] Concerned with Pigment Transformations in the Woolly Aphid Eriosoma lanigerum Hausmann (Hemiptera: Insecta)

1977 ◽  
Vol 30 (3) ◽  
pp. 173 ◽  
Author(s):  
DW Cameron ◽  
WH Sawyer ◽  
VM Trikojus
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Eriosoma Lanigerum ◽  
Purification And Properties ◽  
Woolly Aphid

Dried extracts of woolly aphid were treated with n-butanol, then by chromatography on DEAESephadex A50 and finally by filtration on Sephadex G150 to yield a substantially homogeneous protein catalysing the conversion of the aglucone of protoaphin into xanthoaphin. Traces of lowmolecular- weight contaminants were removed by chromatography on Sephadex G 100. The enzyme, which has a molecular weight of 120000�2000 and a high content of p-structure, was inhibited by naphthoresorcinol. Its glycoprotein nature was indicated by amino acid analysis.

Improved purification, amino acid analysis and molecular weight of homogeneous d-amino acid oxidase from pig kidney

1973 ◽  
Vol 327 (2) ◽  
pp. 266-273 ◽  
Author(s):  
Bruno Curti ◽  
Severino Ronchi ◽  
Umberto Branzoli ◽  
Giuseppina Ferri ◽  
Charles H. Williams
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Pig Kidney
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