Application of a flow system with laser polarimetric automatic detection for molecular exclusion chromatography of carbohydrates

Sugar Tech ◽  
2006 ◽  
Vol 8 (4) ◽  
pp. 229-232 ◽  
Author(s):  
Silvio Naranjo ◽  
Teresa Ceperob ◽  
Victor Fajerb ◽  
Carlos W. Rodriguez ◽  
William Morab ◽  
...  
Keyword(s):  
Flow System ◽  
Automatic Detection ◽  
Exclusion Chromatography ◽  
Molecular Exclusion Chromatography

The Kidney and Fibrinolysis

1970 ◽  
Vol 24 (01/02) ◽  
pp. 026-032 ◽  
Author(s):  
N. A Marsh
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Enzyme System ◽  
Normal Animal ◽  
Fibrinolytic Enzyme ◽  
The Other ◽  
Exclusion Chromatography ◽  
Normal Urine ◽  
Renal Origin ◽  
Molecular Exclusion Chromatography

SummaryMolecular exclusion chromatography was performed on samples of urine from normal and aminonucleoside nephrotic rats. Normal urine contained 2 peaks of urokinase activity, one having a molecular weight of 22,000 and the other around 200,000. Nephrotic urine contained three peaks of activity with MW’s 126,000, 60,000 and 30,000. Plasma activator determined from euglobulin precipitate had a MW. in excess of 200,000. The results indicate that in the normal animal, plasma plasminogen activator does not escape into the urine in substantial quantities but under the conditions of extreme proteinuria there may be some loss through the kidney. The alteration in urokinase output in nephrotic animals indicates a greatly disordered renal fibrinolytic enzyme system.The findings of this study largely support the hypothesis that plasma plasminogen activator of renal origin and urinary plasminogen activator (urokinase) are different molecular species.

scholarly journals Jatropha Neopauciflora Pax Latex Exhibits Wound-Healing Effect in Normal and Diabetic Mice

2021 ◽  
Vol 26 ◽  
pp. 2515690X2098676
Author(s):  
Ana Bertha Hernandez-Hernandez ◽  
Francisco Javier Alarcon-Aguilar ◽  
Mario Garcia-Lorenzana ◽  
Marco Aurelio Rodriguez-Monroy ◽  
Maria Margarita Canales-Martinez
Keyword(s):  
Wound Healing ◽  
Healing Process ◽  
Wound Healing Process ◽  
Diabetic Mice ◽  
Wound Area ◽  
Oral Infections ◽  
Patients With Diabetes ◽  
Exclusion Chromatography ◽  
Wound Healing Effect ◽  
Molecular Exclusion Chromatography

Jatropha neopauciflora is an endemic species of Mexico. Its latex is used to treat wounds, scarring, oral infections, and loose teeth. To date, there are no studies that validate at a morphological level a wound-healing use in diabetes. The present research aimed to evaluate the wound-healing capacity of the latex of J. neopauciflora in the skin of healthy and streptozotocin-induced diabetic mice. Also, a chemical analysis of the latex through molecular exclusion chromatography and HPLC were performed. Male mice ( Mus musculus) of 7-week-old CD1 strain were used. Groups of healthy and diabetic mice were formed. A longitudinal cut of 1 cm was performed on the depilated skin. All treatments were topically applied to the wound area twice a day for ten days. At the end of the experiments, the skin sections were obtained from the wound area and stained with Hematoxylin-Eosin. Then we counted the number of active fibroblasts in all the experimental groups. In normal mice, the latex accelerated the wound-healing process and decreased the number of active fibroblasts, similarly to Recoveron. In diabetic mice, the latex and Recoveron increased the number of active fibroblasts. In normal and diabetic mice, a thin and orderly epidermis was observed. Molecular exclusion chromatography exhibited 58 fractions, 14 of which were subjected to HPLC, to detect catechin, a flavonoid with antioxidant, antimicrobial, and anti-inflammatory properties. J. neopauciflora latex can be useful for wound treatment in patients with diabetes mellitus because it accelerates and promotes the wound-healing process.

Ras GTPase-activating protein physically associates with mitogenically active phospholipids

1991 ◽  
Vol 11 (5) ◽  
pp. 2785-2793
Author(s):  
M H Tsai ◽  
M Roudebush ◽  
S Dobrowolski ◽  
C L Yu ◽  
J B Gibbs ◽  
...  
Keyword(s):  
Mixed Micelles ◽  
Arachidic Acid ◽  
Physical Interaction ◽  
Magnesium Ions ◽  
Gtpase Activating Protein ◽  
Elution Time ◽  
Ras Gtpase ◽  
Exclusion Chromatography ◽  
Tight Association ◽  
Molecular Exclusion Chromatography

The physical interaction between GTPase-activating protein (GAP) and lipids has been characterized by two separate analyses. First, bacterially synthesized GAP molecules were found to associate with detergent-mixed micelles containing arachidonic but not with those containing arachidic acid. This association was detected by a faster elution time during molecular exclusion chromatography. Second, GAP molecules within a crude cellular lysate were specifically retained by a column on which certain lipids had been immobilized. The lipids able to retain GAP on such columns were identical to those which were shown previously to be most active in blocking GAP activity. The association between lipids and GAP was dependent upon magnesium ions. Lipids unable to inhibit GAP activity were also unable to physically associate with GAP. The tight association of GAP with these lipids was predicted by and helps to rationalize their ability to inhibit GAP activity.

scholarly journals Ras GTPase-activating protein physically associates with mitogenically active phospholipids.

1991 ◽  
Vol 11 (5) ◽  
pp. 2785-2793 ◽  
Author(s):  
M H Tsai ◽  
M Roudebush ◽  
S Dobrowolski ◽  
C L Yu ◽  
J B Gibbs ◽  
...  
Keyword(s):  
Mixed Micelles ◽  
Arachidic Acid ◽  
Physical Interaction ◽  
Magnesium Ions ◽  
Gtpase Activating Protein ◽  
Elution Time ◽  
Ras Gtpase ◽  
Exclusion Chromatography ◽  
Tight Association ◽  
Molecular Exclusion Chromatography

The physical interaction between GTPase-activating protein (GAP) and lipids has been characterized by two separate analyses. First, bacterially synthesized GAP molecules were found to associate with detergent-mixed micelles containing arachidonic but not with those containing arachidic acid. This association was detected by a faster elution time during molecular exclusion chromatography. Second, GAP molecules within a crude cellular lysate were specifically retained by a column on which certain lipids had been immobilized. The lipids able to retain GAP on such columns were identical to those which were shown previously to be most active in blocking GAP activity. The association between lipids and GAP was dependent upon magnesium ions. Lipids unable to inhibit GAP activity were also unable to physically associate with GAP. The tight association of GAP with these lipids was predicted by and helps to rationalize their ability to inhibit GAP activity.

Acetylated tubulin associates with the fifth cytoplasmic domain of Na+/K+-ATPase: possible anchorage site of microtubules to the plasma membrane

2009 ◽  
Vol 422 (1) ◽  
pp. 129-137 ◽  
Author(s):  
Guillermo G. Zampar ◽  
María E. Chesta ◽  
Agustín Carbajal ◽  
Natalí L. Chanaday ◽  
Nicolás M. Díaz ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Catalytic Activity ◽  
Molecular Mass ◽  
Cytoplasmic Domain ◽  
Membrane Preparation ◽  
Acetylated Tubulin ◽  
Exclusion Chromatography ◽  
Molecular Exclusion Chromatography

We showed previously that NKA (Na+/K+-ATPase) interacts with acetylated tubulin resulting in inhibition of its catalytic activity. In the present work we determined that membrane-acetylated tubulin, in the presence of detergent, behaves as an entity of discrete molecular mass (320–400 kDa) during molecular exclusion chromatography. We also found that microtubules assembled in vitro are able to bind to NKA when incubated with a detergent-solubilized membrane preparation, and that isolated native microtubules have associated NKA. Furthermore, we determined that CD5 (cytoplasmic domain 5 of NKA) is capable of interacting with acetylated tubulin. Taken together, our results are consistent with the idea that NKA may act as a microtubule–plasma membrane anchorage site through an interaction between acetylated tubulin and CD5.

scholarly journals Identity of ligandin in rat testis and liver

1982 ◽  
Vol 203 (1) ◽  
pp. 193-199 ◽  
Author(s):  
K A Eidne ◽  
R E Kirsch
Keyword(s):  
Reduced Glutathione ◽  
Sodium Dodecyl ◽  
Standard Technique ◽  
Electrophoretic Analysis ◽  
Immunoaffinity Chromatography ◽  
Multiple Forms ◽  
Glutathione S Transferase ◽  
Closely Related Species ◽  
Exclusion Chromatography ◽  
Molecular Exclusion Chromatography

1. One of the main problems in the field of multifunctional proteins such as ligandin is the possibility that multiple forms and isoproteins may exist. Because liver ligandin [GSH (reduced glutathione) S-transferase B] consists of equal amounts of Ya (22 000 Da) and Yc (25 000 Da) subunits, and testis ligandin, prepared by the standard technique of anion-exchange and molecular-exclusion chromatography, contains more Yc subunit than Ya, it has been claimed that testis and liver ligandin are different entities. 2. We purified testis ligandin by immunoaffinity chromatography and have obtained a product identical with liver ligandin (Yc = Ya). This suggests that the differences previously described may be due to contamination of testis ligandin by a closely related species. In fact sodium dodecyl sulphate/polyacrylamide-gel-electrophoretic analysis of testis GSH S-transferases separated by CM-cellulose chromatography showed that GSH S-transferase AA, present in large amounts, migrated in the same region as Yc subunit. 3. Testis ligandin prepared by the standard technique was similar to that reported [Bhargava, Ohmi, Listowsky & Arias (1980) J. Biol. Chem. 255, 724-727] and contained more Yc subunit than Ya. CM-cellulose chromatography of this ‘pure’ preparation revealed significant amounts of GSH S-transferase AA migrating as Yc subunit, in addition to ligandin consisting of equal amounts of Ya and Yc subunits. 4. Our studies show that testis ligandin is identical with liver ligandin. Previously described differences are due to a contaminant identified as GSH S-transferase AA.

scholarly journals Partial purification and properties of cellulase-free alkaline xylanase produced by Rhizopus stolonifer in solid-state fermentation

2005 ◽  
Vol 48 (3) ◽  
pp. 327-333 ◽  
Author(s):  
Antonio José Goulart ◽  
Eleonora Cano Carmona ◽  
Rubens Monti
Keyword(s):  
Solid State ◽  
Wheat Bran ◽  
Solid State Fermentation ◽  
Partial Purification ◽  
Optimum Temperature ◽  
Rhizopus Stolonifer ◽  
Purification And Properties ◽  
Exclusion Chromatography ◽  
Molecular Exclusion Chromatography

Rhizopus stolonifer was cultivated in wheat bran to produce a cellulase-free alkaline xylanase. The purified enzyme obtained after molecular exclusion chromatography in Sephacryl S-200 HR showed optimum temperature as 45º C and hydrolysis pHs optima as pH 6.0 and 9.0. Xylanase presented higher Vmax at pH 9.0 (0.87 µmol/mg protein) than at pH 6.0 and minor Km at pH 6.0 (7.42 mg/mL) than at pH 9.0.

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