• Korean Journal of Food Science and Technology
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• v.25 no.6
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• pp.794-800
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• 1993

A lipid producing yeast was screened from leaves of Albabiscus and was identified as a Rhodotorula graminis SW 214. During the shakining incubation of 8 days at $25^{\circ}C$, the yeast produced extracellular lipids of 7.3g/l of the media. The relative concentration of carbon and nitrogen sources in the media influenced the extracellular lipid production greatly. When with nitrogen sources in the media were almost exhausted for growth of the yeast the sufficient carbon sources, the lipid production proceeded vigorously. Eight days of batch cultivation with 8% glucose, 2.5g/l of yeast extract, $KH_{2}PO_{4}(1g/l)\;MgSO_{4}\;(0.2g/l)$ and pH 6 gave maximum biomass and extracellular lipid production of 8.05g/l and 8.89g/l, respectively. The acid value, saponificatio value, the iodine value, ad the unsaponifiable matter of the extracellular lipids of Rhodotorula graminis SW 214 were 2.6, 534, 5.1 and 2.4, respectively. Lipid was constituted 75.2% triglyceride, 5.9% free fatty acid, 10.8% phospholipid, 4.9% esterified sterol and 3.3% free sterol. Major fatty acids found were 3-hydroxypentadecanoate, 3-hydroxyhexadecanate, trans-9-octadecanate, cis-9-hexadecanate (hydroxy palmitic), 15-methylhexadecanate (oleic), 18-methylno-nadecanate, octadecanate (stearic) and 3-hydroxytridecante.

• Journal of Oral Medicine and Pain
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• v.32 no.4
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• pp.357-364
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• 2007

This experiment was designed to clarify the effect of extracellular glucose on the osteoblasts and periodontal ligament cells. The cells were incubated for 24 and 48 hours with ${\alpha}$-MEM including 1,000 mg/L (control group) and 4,500 mg/L (experimental group) of glucose. Then, the expressions of caspase-3, p38 MAPK, JNK-1, and ERK-1 were examined using Elisa assay and Western blot. The results were as follows: 1. The expression of caspase-3 and p38 MAPK was increased by the high extracellular glucose in both cells. 2. The expression of caspase-3 and p38 MAPK was increased greatly in the periodontal ligament cells than the E1 cells by the high extracellular glucose. 3. The expression of JNK-1 was increased by the high extracellular glucose in both cells. 4. The expression of ERK-1 was not changed by the high extracellular glucose in both cells. These results suggest that extracellular glucose at high concentrations may inhibit the periodontal regeneration process increasing cellular apoptosis. And p38 MAPK and JNK-1 pathway may be the most responsible intracellular pathway rather than ERK-1.

• Journal of Life Science
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• v.20 no.5
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• pp.683-690
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• 2010

The yeast strains of Saccharomyces diastaticus produce one of three isozymes of an extracellular glucoamylase I, II or III, a type of exo-enzyme which can hydrolyse starch to generate glucose molecules from non-reducing ends. These enzymes are encoded by the STA1, STA2 and STA3 genes. Another gene, sporulation-specific glucoamylase (SGA), also exists in the genus Saccharomyces which is very homologous to the STA genes. The SGA has been known to be produced in the cytosol during sporulation. However, we hypothesized that the SGA is capable of being secreted to the extracellular region because of about 20 hydrophobic amino acid residues at the N-terminus which can function as a signal peptide. We expressed the cloned SGA gene in S. diastaticus YIY345. In order to compare the biochemical properties of the extracellular glucoamylase and the SGA, the SGA was purified from the culture supernatant through ammonium sulfate precipitation, DEAE-Sephadex A-50, CM-Sephadex C-50 and Sephadex G-200 chromatography. The molecular weight of the intact SGA was estimated to be about 130 kDa by gel filtration chromatography with high performance liquid chromatography (HPLC) column. Sodium dedecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed it was composed of two heterogeneous subunits, 63 kDa and 68 kDa. The deglycosylation of the SGA generated a new 59 kDa band on the SDS-PAGE analysis, indicating that two subunits are glycosylated but the extent of glycosylation is different between them. The optimum pH and temperature of the SGA were 5.5 and $45^{\circ}C$, respectively, whereas those for the extracellular glucoamylase were 5.0 and $50^{\circ}C$. The SGA were more sensitive to heat and SDS than the extracellular glucoamylase.

• Journal of Microbiology
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• v.40 no.1
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• pp.26-32
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• 2002

From the culture supernatant of the psychrotrophic strain of Bacillus amyloliquefaciens an extracellular serine protease was purified to apparent homogeneity by successive purification steps using QAE-Sephadex, SP-Sephadex and Sephacryl S-100 column chromatography. The pretense is monomeric, with a relative molecular mass of 23,000. It is inhibited by the serine protease inhibitor phenylmethylsulfonyl fluoride, but not by EDTA. The enzyme is most active at pH 9-10 and at $45^{\circ}C$, although it is unstable at $60^{\circ}C$.

• Proceedings of the Korean Biophysical Society Conference
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• 1999.06a
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• pp.68-68
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• 1999

Extracellular A TP is known to function as a neurotransmitter and as a modulator in the variety of cell types. In PC12 cells, extracellular A TP elevates [Ca$\^$2＋/]j through receptor-operated Ca$\^$2＋/ channels and through the activation of phospholipase C, thereby facilitating the secretion of neurotransmitters.(omitted)

• Korean Journal of Microbiology
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• v.24 no.1
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• pp.32-37
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• 1986

In fermentation studies it revealed that Streptomyces sp. SMF 3001 started to synthesize extracellular alkaline protease from early exponential phase of cell growth. The biosynthesis of the alkaline protease was greatly induced by skim milk as a sola nitrogen source and further stimulation was observed under inorganic sulphur limited culture. However, it was found that the biosynthesis was apparently repressed by $NH_4^+$ and free amino acids, specially by cysteine. It was considered that the strain SMF 301 of Streptomyces sp. would produce the alkaline protease for the uptake of sulphur compounds from protein contained in the culture broth.

• Proceedings of the PSK Conference
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• 2003.10a
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• pp.100-101
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• 2003

Cell-cell and cell-matrix interaction is clearly required for metazoans not only to hold their cells together but also to conduct more sophisticated biological processes. Each cell has adhesion molecules on its cell membrane to link extracellular matrix and adjacent cells to the intracellular cytoskeleton, and also to transduce signals. In complex metazoans, information is transmitted from one cell to another by mechanisms such as direct intercellular communication, soluble signal molecules among distant cells, and local cellular environments formed by highly specialized extracellular matrix. (omitted)

• Journal of Life Science
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• v.19 no.5
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• pp.561-565
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• 2009

Human Tissue factor is an essential enzyme activator that forms a catalytic complex with factor VII/ VIIa, and catalyzes both the extrinsic and intrinsic blood coagulation cascades. The extracellular domain of human tissue factor is responsible for association with the biological partner. The efficient procedures for preparing biologically active human tissue factor are essential for the preclinical and clinical studies with coaguligands. An expression vector in Escherichia coli has been constructed to direct the production of extracellular human tissue factor without a fusion protein or a $His_6$ at the N-terminus. The recombinant human tissue factor was expressed in large amounts as a non-native state in E. coli. The recombinant protein was simply renatured during the DEAE-sephacel chromatographic purification procedure. Our expression and purification system does not require a protease treatment or an additional chromatographic step to remove a fusion contaminant, which provides a very useful alternative to conventional expression systems for the production of human tissue factor.

• BMB Reports
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• v.45 no.3
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• pp.159-164
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• 2012

CD99 is known to be involved in the regulation of cell-cell adhesion. However, it remains unclear whether CD99 controls cell-extracellular matrix adhesion. In this study, the effects of CD99 activation on cell-extracellular matrix adhesion were investigated. It was found that engagement of CD99 with the stimulating antibody YG32 downregulated the adhesion of MCF-7 cells to fibronectin, laminin and collagen IV in a dose-dependent manner. The CD99 effect on cell-ECM adhesion was inhibited by overexpression of the dominant negative form of CD99 or CD99 siRNA transfection. Treatment of cells with $Mn^{2+}$ or by ${\beta}_1$ integrin-stimulating antibody restored the inhibitory effect of CD99 on cell-ECM adhesion. Cross-linking CD99 inactivated ${\beta}_1$ integrin through conformational change. CD99 activation caused dephosphorylation at Tyr-397 in FAK, which was restored by the ${\beta}_1$ stimulating antibody. Taken together, these results provide the first evidence that CD99 inhibits cell-extracellular matrix adhesion by suppressing ${\beta}_1$ integrin affinity.

• Journal of Forest and Environmental Science
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• v.24 no.1
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• pp.53-59
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• 2008

Extracellular enzyme activities of Fomitopsis palustris were determined by the particle sizes, culture periods and concentrations of wood particle substrate which was mixture of 4 domestic coniferous woods, such as Pinus densiflora, Larix leptolepsis, Pinus koraiensis, and Pinus rigida. The results showed that the culture conditions had an effect on the secretion of most of the extracellular enzymes from Fomitopsis palustris in the mixed wood particle substrate. :The optimal culture conditions for enzyme activities were 80~100 mesh in wood particle size, 7.5% in concentrations of wood substrate, and 4~8 weeks in culture period.