L Boross
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Explore the profile of L Boross including associated specialties, affiliations and a list of published articles.
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37
Citations
74
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Recent Articles
1.
Deer K, Nemcsok J, Boross L, Szajani B
Fish Physiol Biochem
. 2013 Nov;
8(1):79-83.
PMID: 24221900
The effects of paraquat (PQ; 1,1'-dimethyl-4,4'-bipyridylium dichloride) treatment were investigated in carp, silver carp and wels. The serum glutamic-oxalacetic transaminase (GOT; L-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1.) level was enhanced by...
2.
Boross L, Kosary J, Sisak C, Szajani B
J Biotechnol
. 1998 Dec;
66(1):69-73.
PMID: 9866860
Catalytic properties and conformational stability of aminoacylase (N-acylamino acid amidohydrolase, EC 3.5.1.14) were studied in water-N,N-dimethylformamide (DMF) and water-dioxane solvent mixtures. Beside the prompt inhibition the solvents caused further inactivation...
3.
Kosary J, Cseke E, Boross L
Pharmazie
. 1995 Jul;
50(7):489-90.
PMID: 7675893
The possibilities of exact measuring the effect of metal ions on the activity of phosphofructokinase (PFK) by means of both a heat inactivation and an auxiliary enzyme system were studied....
4.
Buzas Z, Dallmann K, Boross L, Szajani B, Horvath G
Acta Biochim Biophys Hung
. 1990 Jan;
25(1-2):9-16.
PMID: 2130575
Factors influencing the operation of a vertical bioreactor segmented with perforated plates supporting immobilized yeast cells were studied. It was found that the most important factors are the length-diameter (L/D)...
5.
Horvath L, Abraham M, Boross L, Szajani B
Appl Biochem Biotechnol
. 1989 Dec;
22(3):223-35.
PMID: 2556962
Pig muscle aldolase was covalently attached to a silica-based support possessing aldehyde functional groups. The activity of the immobilized enzyme was 37 U/g solid, and the specific activity calculated on...
6.
Abraham M, Boross L, Szajani B
Prikl Biokhim Mikrobiol
. 1988 Jul;
24(4):499-503.
PMID: 2847142
Glucose oxidase (beta-D-glucose: oxygen 1-oxidoreductase, EC 1.1.3.4) was covalently coupled to silica-based supports containing aldehyde functional groups. The activity of the immobilized enzyme was about 1000 U/g support. The optimum...
7.
Simon L, Kotorman M, Boross L, Szajani B
Acta Biochim Biophys Hung
. 1988 Jan;
23(3-4):247-54.
PMID: 3150193
Some glycolytic enzymes (lactate dehydrogenase, pyruvate kinase, enolase and phosphoglyceromutase) were immobilized on a polyacrylamide-type bead polymer containing carboxylic functional groups activated by water-soluble carbodiimide. The immobilized enzymes were used...
8.
Kotorman M, Simon L, Szajani B, Boross L
Biotechnol Appl Biochem
. 1986 Feb;
8(1):53-9.
PMID: 3828081
Pig muscle lactate dehydrogenase (L-lactate:NAD oxidoreductase, EC 1.1.1.27) was covalently immobilized on polyacrylamide beads containing carboxylic functional groups activated by water-soluble carbodiimide. The effects of immobilization on the catalytic properties...
9.
Abraham M, Kirstein D, Scheller F, Boross L
Acta Biochim Biophys Hung
. 1986 Jan;
21(3):225-8.
PMID: 3099523
A coupled enzymatic method elaborated for NAD+-dependent dehydrogenases has been adapted for NADP+-dependent isocitrate dehydrogenase, in combination with amperometric measurements. The isocitrate dehydrogenase activity dependent linearly on the isocitrate concentration...
10.
Simon L, Kotorman M, Szajani B, Boross L
Appl Biochem Biotechnol
. 1985 Jun;
11(3):195-205.
PMID: 4051478
Rabbit muscle pyruvate kinase was immobilized by covalent attachment to a polyacrylamide support (Akrilex C) containing carboxylic functional groups. As a result of immobilization, the pH optimum for catalytic activity...