SVIBOR - Papers quoted in CC - project code: 4-07-024
MINISTRY OF SCIENCE AND TECHNOLOGY
Strossmayerov trg 4, HR - 10000 ZAGREB
tel.: +385 1 459 44 44, fax: +385 1 459 44 69
E-mail: ured@znanost.hr
SVIBOR - Collecting Data on Projects in Croatia
Papers quoted in Current Contents on project 4-07-024
Quoted papers: 11
Other papers: 40
Total: 51
Title: Saccharomyces cerevisiae a- and alpha-agglutinin:
characterization of their molecular interaction
- Authors:
- Cappellaro, Corinna
- Hauser, Karin
- Mrša, Vladimir (39525)
- Watzele, Manfred
- Watzele, Gabriele
- Gruber, Claudia
- Tanner, Widmar
Journal: The EMBO Journal
Number: 13
Volume: 10
Year: 1991
Pages: from 4081 to 4088
Language: engleski
Summary: Saccharomyces cerevisiae a-agglutinin has been isolated,
purified and its gene was cloned by PCR via peptide sequences. It was shown
that the protein forms in vitro specific 1:1 complex withalpha-agglutinin.
Pretreatment of alpha-agglutinin, but not of a-agglutinin with
diethylpyrocarbonate prevents the formation of the complex. The active
region of alpha agglutinin for the reaction with a-agglutinin was defined.
Carbohydrate chains of either agglutinin seem not to be essential for their
interaction.
Keywords: DNA sequence of a-agglutinin, protein-protein interactions, diethylpyrocarbonate inhibition
Title: Activation of the weakly regulated PHO8 promoter in S.
cerevisiae: chromatin transition and binding sites for the positive
regulatory protein PHO4
- Authors:
- Barbarić, Slobodan (2072)
- Fascher, Klaus
- Horz, Wolfram
Journal: Nucleic Acids Research
Number: 5
Volume: 20
Year: 1992
Pages: from 1031 to 1038
Language: engleski
Summary: S. cerevisiae alkaline phosphatase (PHO8) is regulated by
the phosphate concentration in the medium via several positive and negative
regulatory proteins, Pho4 playing the central role. It was shown that under
conditions of PHO8 repression, there is a highly ordered chromatin
structure at the PHO8 promoter. In vitro footprinting revealed two Pho4
binding sites at PHO8 promoter, each within one hypersensitive site. Upon
derepression of PHO8, the chromatin structure changes significantly so that
the two hypersensitive sites containing Pho4 binding sites merge. This
transition is Pho4 dependent.
Keywords: yeast alkaline phosphatase, gene expression, chromatin structure
Title: Expression, glycosylation and secretion of yeast acid
phosphatase in hamster BHK cells
- Authors:
- Reljić, Rajko
- Barbarić, Slobodan (2072)
- Ries, Blanka (41020)
- Buxton, Roger
- Hughes, Roger Colin
Journal: Glycoconjugate Journal
ISSN: 0282-0080
Volume: 9
Year: 1992
Pages: from 39 to 44
Language: engleski
Summary: The gene PHO5, coding for one of the repressible acid
phosphatases of the yeast S. cerevisiae, has been expressed at high
efficiency in baby hamster kidney (BHK) cell line. The recombinant acid
phosphatase was secreted in active form and its size suggested the presence
of 2-3 asparagine linked glycan chains. Analysis by sequential lectin
affinity chromatography of acid phosphatase glycopeptides showed that the
glycans were predominantly of the 2.2.4 triantennary and tetraantennary
complex type. These adta suggest that the extensive glycosylation of yeast
acid phosphatase which contains 8 carbohydrate chains, is not essential for
secretion and expression of enzymatic activity of the transfected gene
product.
Keywords: yeast acid phosphatase, glycosylation, transfection, BHK cells
Title: New chromogen for assay of glucose in serum
- Authors:
- Reljić, Rajko
- Ries, Mihael
- Anić, Nataša
- Ries, Blanka (41020)
Journal: Clinical Chemistry
Number: 4
Volume: 38
Year: 1992
Pages: from 522 to 525
Language: engleski
Summary: A colorimetric assay for glucose determination in human
serum with the use of chromogen 2-amino-4-hydroxybenzene sulphonic acid,
glucose oxidase, and peroxidase , is described. A single working reagent is
used, and the reaction is completed within 10 minutes at 37 deg. C. The
absorbance of the yellow reaction product is measured at 415 nm, and a
blank sample measurement is not needed. The results of the recommended
procedure corelated well with those of the phenol/4-aminoantipyrine method.
Keywords: glucose concentration determination, enzymatic methods
Title: Binding of Saccharomyces cerevisiae extracellular proteins
to glucan
- Authors:
- Mrša, Vladimir (39525)
- Ugarković, Tatjana
- Barbarić, Slobodan (2072)
Journal: Archives of Biochemistry and Biophysics
Number: 2
ISSN: 0003-9861
Volume: 296
Year: 1992
Pages: from 569 to 574
Language: engleski
Summary: Interactions of S. cerevisiae cell wall proteins with
purified yeast glucan were studied. Using the beta-glucanase as the model
cell wall protein, strong binding to glucan was demonstrated at pH lower
than 7. It was also found that most other cell wall proteins, as well as
intracellular proteins, reacted with glucan in the same way, showing that
these interactions were rather nonspecific. Soluble periplasmic proteins,
invertase and acid phosphatase, failed to react with glucan , indicating
that these proteins have certain structural features preventing their
interactions with glucan.
Keywords: S. cerevisiae cell wall, cell wall proteins, yeast glucan, protein-glucan interactions
Title: Purification and characterization of the Saccharomyces
cerevisiae BGL2 gene product, a cell wall endo-bata-1,3-glucanase
- Authors:
- Mrša, Vladimir (39525)
- Klebl, Franz
- Tanner, Widmar
Journal: Journal of Bacteriology
Number: 7
ISSN: 0021-9193
Volume: 175
Year: 1993
Pages: from 2102 to 2106
Language: engleski
Summary: One of the major proteins of the Saccharomyces cerevisiae
cell wall, a beta-glucanase, has been isolated and purified to
homogeneity.It was found that the enzyme was an endo-beta-1,3-glucanase,
and not an exoglucanase as reported previously. The analisys of the
glucanase structure revealed that the potential N-glycosylation site at
Asn284, but not that at Asn202, was used for glycosylation. The
overproduction of the beta-glucanase from the high-copy-number plasmid
brought about the significant decrease in the growth rate of transformed
yeast cells.
Keywords: yeast cell wall, beta-glucanase
Title: Specific dephosphorylation of phpsphopeptides by the yeast
alkaline phosphatase encoded by PHO8 gene
- Authors:
- Donella-Deana, Arianna
- Ostojić, Sanja
- Pinna, Lorenzo A.
- Barbarić, Slobodan (2072)
Journal: Biochimica et Biophysica Acta
ISSN: 0167-4889
Volume: 1177
Year: 1993
Pages: from 221 to 228
Language: engleski
Summary: Partially purified nonspecific phosphate-repressible
alkaline phosphatase from S. cerevisiae necoded by PHO8 gene efficiently
dephosphorylates phosphohistones and a variety of phosphopeptides. The pho8
mutant, constructed by disruption of the chromosomal counterpart of the
PHO8 gene, is lacking the phosphatase activity toward phosphopeptides. Its
specificity towards synthetic peptides and insensitivity to specific
inhibitors and activators indicate that alkaline phosphatase differs from
both Ser/thr- and Tyr-specific protein phosphatases.
Keywords: Phosphohistone, phosphopeptide, dephosphorylation (Saccharomyces cerevisiae)
Title: Detection of exo-beta-1,3-glucanase activity in
polyacrylamide gels after electrophoresis under deneturing or nondeneturing
conditions
- Authors:
- Vargić, Tamara
- Mrša, Vladimir (39525)
- Mrša, Vladimir (39525)
Journal: Electrophoresis
Number: 7
ISSN: 0173-0835
Volume: 15
Year: 1994
Pages: from 903 to 906
Language: engleski
Summary: A method for visualization of exo-beta-1,3-glucanase
activity in polyacrylamide gels is presented. The procedure consists of the
enzyme reaction in the gel with the substrate alpha-naphtylglucopyranoside,
and the susequent staining of obtained alpha-naphtol with dyes Fast Red B,
or Fast Blue BB. The procedure is applicable for the standard Laemmli
discontinuous electrophoresis system, even in the presence of sodium
dodecyl sulphate, as well as for the electrophoresis in linear gradients of
the polyacrylamide concentration.
Keywords: exoglucanase, zymograms, activity staining of electrophoresis
Title: Cross-linking, stabilization and detection of
glycoproteins
- Authors:
- Barbarić, Slobodan (2072)
- Česi, Vlasta (116565)
- Delaš, Ivančica
- Gebauer, Branka
- Heimgartner, Urs
- Kozulić, Branko
- Mosbach, Klaus
Journal: Acta Pharmaceutica
Number: 4
ISSN: 1330-0075
Volume: 44
Year: 1994
Pages: from 353 to 365
Language: engleski
Summary: Several dihydrazides were used to cross-link, inter- and
intramolecularly, many different glycoenzymes and immunoglobulines. The
process was employed for studying the spatial proximity of sugar chains in
glycoprotein molecules, and the stability of glycoenzymes. The obtained
results, especially those with immunoglobulines, indicate that the method
is applicable in spatial arrangements of sugar chains. Besides, it was
found that some glycoenzymes could be greatly stabilized by cross-linking
their oxidized carbohydrate chains with bifunctional cross-linkers.
Keywords: Oxidized glycoproteins, hydrazide reagents
Title: Enzymatic Properties of the Xylanase Preparation from
Thermomyces lanuginosus
- Authors:
- Cesar, Tatjana
- Mrša, Vladimir (39525)
Journal: Croatica Chemica Acta
Number: 3
ISSN: 0011-1643
Volume: 68
Year: 1995
Pages: from 675 to 681
Language: engleski
Summary: Xylanase preparation obtained by submersed fermentation of
Thermomyces lanuginosus was characterized. The preparation was apparently
devoid of proteins as shown by electrophoresis. The enzyme exhibited the
highest activity at pH about 7.0, and was stable for 96 hours at pH between
5.0 and 9.0. Dithiobis-2-nitrobenzoic acid, p-hydroxymercuribenzoic acid
and Hg2+ ions completely inhibited the enzyme, while Mn2+, Fe2+ and
beta-mercaptoethanol enhanced the xylanase activity.
Keywords: Xylanase - Thermomyces lanuginosus
Title: Structure of the Saccharomyces cerevisiae Cell Wall
- Authors:
- Vuković, Renata
- Mrša, Vladimir (39525)
Journal: Croatica Chemica Acta
Number: 3
ISSN: 0011-1643
Volume: 68
Year: 1995
Pages: from 597 to 605
Language: engleski
Summary: To elucidate the structure of the Saccharomyces cerevisiae
cell wall, intermolecular interactions responsible for the constitution of
the cell wall were studied. Results revealed protein-glucan,
protein-chitin, glucan-chitin, and glucan-glucan interactions. Mannan
chains reacted neither with proteins nor with other polysaccharides. Intact
cell walls were found to bind proteins approaching the wall from the
inside, but not those reaching the cell wall from the outer side,
suggesting a marked asymmetry of the wall having an outer mannan layer, and
an inner glucan network.
Keywords: Saccharomyces cerevisiae cell wall, glucan, mannan, chitin, protein - carbohydrate interactions
Information: svibor@znanost.hr
