Characterization of the organic fraction of an uncomposted and composted sewage sludge by isoelectric focusing and gel filtration

1992 ◽  
Vol 13 (2) ◽  
pp. 112-118 ◽  
Author(s):  
C. Garc�a ◽  
T. Hern�ndez ◽  
F. Costa ◽  
B. Ceccanti ◽  
C. Dell'Amico
Keyword(s):  
Sewage Sludge ◽  
Isoelectric Focusing ◽  
Gel Filtration ◽  
Organic Fraction ◽  
Composted Sewage Sludge

scholarly journals Solubilization and characterization of pellet-associated human brain α-L-fucosidase activity

1985 ◽  
Vol 229 (3) ◽  
pp. 679-685 ◽  
Author(s):  
R L Hopfer ◽  
J A Alhadeff
Keyword(s):  
Human Brain ◽  
Isoelectric Focusing ◽  
Human Liver ◽  
Gel Filtration ◽  
Compelling Evidence ◽  
Supernatant Fluid ◽  
Ph Optimum ◽  
Triton X ◽  
Soluble Supernatant

The pellet-associated portion of human brain alpha-L-fucosidase (which represents approx. 20% of the homogenate activity) was solubilized with 0.5% (w/v) Triton X-100, characterized with regard to several properties and compared with the corresponding properties of the soluble supernatant-fluid enzyme in an attempt to find a second alpha-L-fucosidase in human brain. The solubilized and soluble alpha-L-fucosidase activities exhibited complete stability after storage at 2-4 degrees C for up to 29 days, comparable thermostability after preincubation at 50 degrees C, comparable apparent Km values (0.07-0.08 mM) for 4-methylumbelliferyl alpha-L-fucopyranoside, comparable hydrophobicity, comparable isoelectric-focusing profiles (six major forms, with pI values between 4.5 and 5.8) and comparable immunoprecipitation curves (with the IgG fraction of antisera prepared against human liver alpha-L-fucosidase). Differences in three properties were found between solubilized and soluble alpha-L-fucosidase activities: the solubilized activity was less stable to storage at −20 degrees C, had a 0.5-pH-unit neutral shift in its pH optimum (6.0) and had smaller Mr forms after gel filtration on Sephadex G-200. The overall results indicate that the pellet-associated and soluble portions of human brain alpha-L-fucosidase are quite similar in most of their properties. Thus there is still no compelling evidence for the existence of a second mammalian alpha-L-fucosidase.

scholarly journals Characterization of Cellulases and Related Enzymes by Isoelectric Focusing, Gel Filtration, and Zone Electrophoresis. I. Aspergillus Enzymes.

1967 ◽  
Vol 21 ◽  
pp. 937-944 ◽  
Author(s):  
Elisabeth Ahlgren ◽  
Karl-Erik Eriksson ◽  
Olof Vesterberg ◽  
Å. Åkeson ◽  
H. Theorell ◽  
...  
Keyword(s):  
Isoelectric Focusing ◽  
Gel Filtration ◽  
Zone Electrophoresis

Separation and Characterization of Two Fibrinolytic Inhibitors from Human Placenta

1971 ◽  
Vol 25 (03) ◽  
pp. 580-589 ◽  
Author(s):  
M Uszynski ◽  
U Abildgaard
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Isoelectric Focusing ◽  
Basic Protein ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Coagulation Inhibitor ◽  
Tissue Thromboplastin

SummaryProcedures for the separation of two inhibitors of the activation of plasminogen to plasmin by urokinase are described. Tissue thromboplastin was removed by adsorption to Al(0H)3 gel followed by ultracentrifugation. Plasminogen, plasminogen activator, a coagulation inhibitor and hemoglobin were removed by ion exchange chromatography (CM- or DEAE-Sephadex with NaCl gradients). The minor UK inhibitor is a relative basic protein with a pI of about 5.8. The major inhibitor was purified further by isoelectric focusing, preparative electrophoresis in polyacrylamide gel, and gel filtration. This inhibitor has α1-motility, the pI is about 5.2, and the molecular weight about 100,000. It inactivates urokinase progressively, but does not inhibit streptokinase, plasmin or thrombin.

Partial characterization of an extracellular β-fructofuranosidase from Clavibacter michiganensis subspecies sepedonicus

1998 ◽  
Vol 44 (9) ◽  
pp. 852-865 ◽  
Author(s):  
Debra Baer ◽  
Alan R White ◽  
Neil C Gudmestad
Keyword(s):  
Isoelectric Focusing ◽  
Culture Medium ◽  
Gel Filtration ◽  
Clavibacter Michiganensis ◽  
Sucrase Activity ◽  
Phytopathogenic Bacteria ◽  
Enzyme Preparations ◽  
Phase Partition ◽  
Clavibacter Michiganensis Subsp

Clavibacter michiganensis subsp. sepedonicus, a phytopathogenic bacteria isolated from potato and sugar beet, produces an extracellular β-fructofuranosidase inducible by sucrose, glucose, fructose, mannose, galactose, and raffinose. This enzyme, also known as invertase or sucrase (β-D-fructofuranoside fructohydrolase, EC 3.2.1.26), is found in the supernatant of C. michiganensis subsp. sepedonicus broth cultures. The maximal sucrase activity in the culture medium was observed after 96 h of incubation. Very little of this enzyme was associated with the cells. The enzymatic activity in the supernatant was concentrated by ethanol precipitation and further purified by a procedure that included polyethylene glycol 1450 aqueous phase partition and preparative isoelectric focusing as the main steps. Enzyme preparations were separated into two fractions (I and II) by gel-filtration chromatography. The preparative isoelectric focusing of the native enzyme showed that most activity was concentrated in the pI range of 4.0-5.0. The enzyme hydrolyzed sucrose, raffinose, and stachyose but hydrolyzed very little inulin, levan, cellobiose, lactose, maltose, or melezitose. The enzyme demonstrated glucosyltransferase activity toward [U-14C]sucrose, cleaving the disaccharide into glucose and fructose, with a small amount incorporated into a trisaccharide.Key words: levansucrase, glucosyltransferase, sucrase, dextransucrase, Solanum tuberosum

scholarly journals Characterization of Glucoamylase from Rhizopus by Isoelectric Focusing and Gel Filtration

1976 ◽  
Vol 29 (8) ◽  
pp. 439-444 ◽  
Author(s):  
Takashi HANDA ◽  
Shigeru MINEKI ◽  
Hiroshi IIZUKA
Keyword(s):  
Isoelectric Focusing ◽  
Gel Filtration
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