The major glycoprotein in germinating bean seeds

1971 ◽  
Vol 49 (12) ◽  
pp. 2107-2111 ◽  
Author(s):  
David Racusen ◽  
Murray Foote
Keyword(s):  
Molecular Weight ◽  
Phaseolus Vulgaris ◽  
Total Protein ◽  
Soluble Protein ◽  
Deae Cellulose ◽  
Apparent Molecular Weight ◽  
Disc Electrophoresis ◽  
Total Soluble Protein ◽  
Combined Analysis

Bean seeds (Phaseolus vulgaris) yielded a soluble glycoprotein that accounted for about 35% of the total protein as determined by combined analysis with DEAE-cellulose and disc electrophoresis. Germination for up to 114 h had little effect on this glycoprotein or on the total soluble protein. The glycoprotein had an apparent molecular weight of 130 000 (6.1 S), contained 14.7% nitrogen, and yielded mannose, glucosamine, and some pentose upon hydrolysis.

Purification of Ristocetin Willebrand Factor (RWF)

1975 ◽  
Author(s):  
J. D. Olson ◽  
D. N. Fass ◽  
W. J. Brockway ◽  
E. J. W. Bowie ◽  
K. G. Mann
Keyword(s):  
Molecular Weight ◽  
Factor Viii ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Apparent Molecular Weight ◽  
Amino Sugar ◽  
Procoagulant Activity ◽  
Factor Viii Inhibitor ◽  
Induced Aggregation

A component required for the ristocetin-induced aggregation of platelets was isolated in yields of 20-30% from pooled human and porcine plasma by cryoethanol concentration of the RWF, after removal of the vitamin K dependent coagulation factors on barium citrate. The concentrate was further purified using gel filtration (4% agarose) and ion exchange (DEAE-cellulose) chromatography. Sodium dodecyl sulfate polyacrylamide gels of the isolated factor indicated an apparent molecular weight of greater than 500,000. After reduction of RWF with mercaptoethanol, a single band is resolved with an apparent molecular weight of 230,000. The purified component had no factor VIII procoagulant activity and did not compete for the activity of naturally occurring factor VIII inhibitor (human). Antisera raised in rabbits directed against the purified component inhibited the RWF activity but not the factor VIII procoagulant activity of plasma. Amino acid analysis indicated the presence of all normal amino acids and failed to detect any amino sugar. Analysis of lipid revealed a significant amount of lipid composed of mono, di and triglycerides, cholesterol, cholesterol esters and free fatty acid, with small portions of phospholipids.

scholarly journals USE OF PHYSIOLOGICAL-BIOCHEMICAL, CELLULAR AND SUB-CELLAR CHARACTERISTICS OF BETULA PENDULA AS MARKERS OF SEED GERMINATION AND MONITORING TERRITORY POLLUTION

2019 ◽  
Vol 16 (32) ◽  
pp. 1034-1044
Author(s):  
T. V. VOSTRIKOVA ◽  
O. A. ZEMLYANUKHINA ◽  
V. N. KALAEV
Keyword(s):  
Seed Germination ◽  
Total Protein ◽  
Soluble Protein ◽  
Betula Pendula ◽  
Anthropogenic Pollution ◽  
Total Soluble Protein ◽  
Anthropogenic Pressure ◽  
Seed Progeny ◽  
Germination Ability ◽  
Weeping Birch

The amount of total soluble protein cytogenetic indices, germination ability in the seed progeny of Betula pendula in areas with different levels of anthropogenic pollution was studied. The seed progeny of Betula pendula has an increased germination ability and total protein in areas with low pollution levels as compared to the control group (seeds collected in the ecologically clean territory) and to the same parameters for the areas with high levels of anthropogenic pressure. A high positive correlation was established between seed germination and the amount of total soluble protein. The parameter “amount of total protein” is characterized as a marker of seed germination, which determines the possibility of their germination. Cytogenetic parameters (mitotic activity, percentage ratio of cell number at mitosis stages, level of mitosis pathologies, level of cells with persistent nucleoli at metaphase - anaphase mitosis stage) of seed seedlings of weeping birch were studied as marker signs of anthropogenic pollution of territories. Relations between cytogenetic and biochemical characteristics were found. The impact of the environment, caused mainly by heavy metal pollution, on birch trees and their seed progeny, can be defined as hormesis by biochemical and cytogenetic indices. A comprehensive study of cytogenetic and biochemical parameters can allow a quick and adequate evaluation of the seed quality of unknown origin which is especially important for plant industry and forestry as it allows selecting stable planting material and for the collection of material for pharmacognostic purposes in areas with different ecological pressure. Determining cytogenetic indices and the amount of total protein allows forecasting the germination capacities and germination abilities of the seeds of the weeping birch.

Isolation and Characterization of a Pancreatic Elastase from Plasma of Patients with Acute Pancreatitis

1982 ◽  
Vol 62 (3) ◽  
pp. 321-328 ◽  
Author(s):  
Naotika Toki ◽  
Sumiyoshi Takasugi ◽  
Hiroyuki Sumi
Keyword(s):  
Acute Pancreatitis ◽  
Specific Activity ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Apparent Molecular Weight ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Isolation And Characterization ◽  
Bean Trypsin Inhibitor

1. An elastase-like enzyme in plasma of patients with acute pancreatitis was purified by DEAE-cellulose column chromatography and polyacrylamide-gel disc electrophoresis. 2. In this way 0.24 mg of purified enzyme with a specific activity of 3.94 succinyl-l-alanyl-l-alanyl-l-alanyl-p-nitroanilide units/mg of protein was obtained from 10 ml of plasma. 3. The purified material was homogeneous as ascertained by sodium dodecyl sulphate/polyacrylamide-gel disc electrophoresis and had an apparent molecular weight of 24 000 as measured by gel filtration on Sephadex G-100. 4. This enzyme hydrolysed denatured casein and Congo Red—elastin as well as succinyl-l-alanyl-l-alanyl-l-alanyl-p-nitroanilide. Its amidolytic activity was inhibited by soya bean trypsin inhibitor, but not by aprotinin. 6. We propose that an elastase-like enzyme, probably different from elastase 1 or elastase 2, is liberated from the pancreas into blood during acute pancreatitis and becomes combined with α2-macroglobulin.

scholarly journals The separation and characterization of marmoset kidney β-d-galactosidase and β-d-glucosidase

1977 ◽  
Vol 167 (3) ◽  
pp. 765-773 ◽  
Author(s):  
R J Pierce ◽  
R G Price
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Apparent Molecular Weight ◽  
Exchange Chromatography ◽  
Starch Gel Electrophoresis ◽  
Lysosomal Fraction ◽  
Glucosidase Activity ◽  
Starch Gel

beta-D-Galactosidase and beta-D-glucosidase activities were determined in homogenates of marmoset kidney by using the appropriate 4-methylumbelliferyl glycoside, beta-D-Galactosidase activity was separated into two main components by ion-exchange chromatography on DEAE-cellulose, starch-gel electrophoresis, isoelectric focusing and gel filtration on Sephadex G-200. One form designated A had a pI of 5.1, was loosely bound to DEAE-cellulose at pH7.0, remained near the origin on starch-gel electrophoresis at pH 7.0 and had an apparent molecular weight of 160000. The second beta-D-galactosidase component, designated B, was associated with the total beta-D-glucosidase activity, had a pI of 4.3, was firmly bound to DEAE-cellulose, migrated rapidly towards the anode on starch-gel electrophoresis and had an apparent molecular weight of 50000. The optimum pH values of beta-D-galactosidase A and B were 4.5 and 6.0 respectively. beta-D-Galactosidase A was activated by 0.1 M-NaC1 but the activity of the B form was inhibited by 1 M-NaC1 at pH 4.5. beta-D-galactosidase had a bimodal distribution, the A form being recovered in the lysosomal fraction whereas the B form was present in the soluble fraction, as was the major portion of the beta-D-glucosidase activity. The lysosomal and soluble forms were further characterized by DEAE-cellulose chromatography.

scholarly journals Proteinuria in rats in relation to age-dependent renal changes

1980 ◽  
Vol 14 (2) ◽  
pp. 95-101 ◽  
Author(s):  
Jeannette M. Alt ◽  
H. Hackbarth ◽  
F. Deerberg ◽  
H. Stolte
Keyword(s):  
Molecular Weight ◽  
Total Protein ◽  
Plasma Proteins ◽  
Disc Electrophoresis ◽  
Male Rats ◽  
Low Molecular Weight ◽  
Urinary Proteins ◽  
Protein Excretion ◽  
Age Dependent ◽  
Renal Changes

A variety of sex-dependent urinary proteins of low molecular weight, absent in females and in castrated males, can be identified in male rats by disc electrophoresis. In the urine of male rats of age 5·5 months, albumin comprises only 1-2% of the total protein. Albumin excretion increases greatly with age and associated kidney disease. Total protein excretion, however, stays the same or even decreases slightly as the rat ages, due to a loss of low molecular weight, sex-dependent, proteins. These are virtually absent in senescent rats (38 months of age), although total protein excretion rises tenfold in these animals due to high molecular weight plasma proteins passing into the urine; the glomerular filtration rate decreases to 70% of the value measured at 5·5 months of age.

DISTRIBUTION OF THE OESTROGEN-INDUCED PROTEIN AND OF TOTAL PROTEIN BETWEEN ENDOMETRIAL AND MYOMETRIAL FRACTIONS OF THE IMMATURE AND MATURE RAT UTERUS

1974 ◽  
Vol 63 (3) ◽  
pp. 439-449 ◽  
Author(s):  
BENITA S. KATZENELLENBOGEN ◽  
R. E. LEAKE
Keyword(s):  
Total Protein ◽  
Soluble Protein ◽  
New Method ◽  
Total Soluble Protein ◽  
Physiological Effects ◽  
Rat Uterus ◽  
Immature Rat ◽  
Significant Enrichment ◽  
Total Dna ◽  
Preferential Synthesis

SUMMARY Using two methods for preparation of endometrial and myometrial tissue fractions – a new method based on mincing and gentle maceration of the immature rat uterus, or separation by dissection of endometrium and myometrium from the mature uterus – both controlled histologically, we have analysed the distribution of the oestrogen-induced protein (IP), and total protein and DNA in these endometrial and myometrial fractions. Studies with both immature and mature oestrogen-stimulated uteri indicate that IP is synthesized in both the endometrial and myometrial tissues. In the immature uterus, there was a marked enrichment of IP in the endometrial fraction. When macerated for 20 or 50 s, 60–70% of the total IP, 5% of the total DNA, 9% of the total protein, and 24–30% of the total soluble protein were found in the endometrium. This enrichment is shown to be due most likely to preferential synthesis of IP in the endometrium. In contrast, in the mature uterus, there was no significant enrichment of IP in the endometrium. Since IP synthesis is associated with the action of oestrogen on both endometrium and myometrium, and the ultimate physiological effects of oestrogen on the two tissues seem to be different, the divergence of the action of oestrogen in these tissues may occur at some point after IP synthesis.

scholarly journals Polypeptides From Serum Low-Density Lipoproteins of Pigs (Sus Domesticus)

1976 ◽  
Vol 29 (4) ◽  
pp. 301
Author(s):  
CS Walkley ◽  
DR Husbands
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Soluble Protein ◽  
Analytical Ultracentrifugation ◽  
Apparent Molecular Weight ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Protein Chromatography ◽  
The Third ◽  
Sus Domesticus

Low-density lipoproteins floating between densities 1� 006 and 1 . 063 g cm - 3 were isolated by centrifugation of blood serum obtained from 24-h fasted pigs (Sus domesticus). This lipoprotein fraction contained two components with SF 1 . 063 values of 3 . 4 and 2� 3 at 20DC when examined by analytical ultracentrifugation. Delipidation of the lipoprotein yielded 15 % recovery of soluble protein whereas succinylation of the lipoprotein prior to delipidation gave 95 % recovery of soluble protein. Chromatography on Sephadex Gl00 in 8 M urea of these delipidation products yielded three fractions of different sizes which were present in both native and succinylated apoproteins. These fractions from the succinylated apolipoproteins were further characterized. A polypeptide fraction comprising 70 % of the total protein had an apparent molecular weight of 34000 and contained greater amounts of amino acids with hydrophobic side chains than did the second fraction of apparent molecular weight 22000 which contained 15 % of the protein. The third fraction of apparent molecular weight 12 500 contained 15 % of the protein.

scholarly journals Isolation and characterization of tryase, a serine proteinase from rat liver

1981 ◽  
Vol 193 (1) ◽  
pp. 251-259 ◽  
Author(s):  
J Saklatvala ◽  
J S Bond ◽  
A J Barrett
Keyword(s):  
Molecular Weight ◽  
Rat Liver ◽  
Sodium Dodecyl ◽  
Liver Homogenate ◽  
Deae Cellulose ◽  
Serine Proteinase ◽  
Apparent Molecular Weight ◽  
Soya Bean ◽  
Gel Chromatography ◽  
Isolation And Characterization

1. A new serine proteinase, tryase, was isolated from the membrane fraction of a post-nuclear supernatant of rat liver homogenate. The enzyme was solubilized with 1 M-MgCl2 and purified to homogeneity by DEAE-cellulose chromatography and affinity chromatography with soya-bean trypsin inhibitor linked to Sepharose 4B. 2. The enzyme was identified on sodium dodecyl sulphate/polyacrylamide gels by reaction with radiolabelled di-isopropyl phosphorofluoridate. Unreduced its molecular weight was 32 500, reduced it was 28 000. 3. The enzyme readily hydrolysed azocasein and tripeptide nitroanilide substrates with an arginine or lysine residue adjacent to the leaving group. D-Pro-Phe-Arg-NPhNO2 was used routinely (Km = 0.25 mM). Tryase showed little activity on blocked arginine esters or amides. 4. It was inhibited by di-isopropyl phosphorofluoridate, benzamidine, aprotinin, soya-bean and lima-bean trypsin inhibitors, Ile-Leu-Arg-CH2Cl and Phe-Ala-Arg-CH2Cl. It was not inhibited by Tos-Lys-CH2Cl. 5. Subcellular-fractionation studies showed that tryase was associated with particles similar in their sedimentation properties to lysosomes, but, since it was not present in tritosomes, it was not in the classical lysosome. 6. Rat liver contained other neutral proteinases; one of these was a serine proteinase with an apparent molecular weight of 90 000 on gel chromatography.

Resolution of the phosphoenolpyruvate: fructose phosphotransferase system of Escherichia coli into two components; enzyme IIfructose and fructose-induced HPr-like protein (FPr)

1980 ◽  
Vol 58 (10) ◽  
pp. 1144-1146 ◽  
Author(s):  
E. Bruce Waygood
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Membrane Protein ◽  
Deae Cellulose ◽  
Apparent Molecular Weight ◽  
Phosphotransferase System ◽  
Sugar Phosphorylation

A protein that substitutes for histidine-containing protein (HPr) in the phosphoenolpyruvate: fructose phosphotransferase system has been found in Escherichia coli grown on fructose. The impure preparation of the fructose-induced HPr-like protein (FPr) appears to be an extrinsic membrane protein which differs from HPr on the basis of its apparent molecular weight (45 000 vs. 9600, respectively), its affinity for DEAE-cellulose and its ability to promote sugar phosphorylation which is specific for fructose, rather than for glucose.

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