• Journal of Plant Biology
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• v.32 no.4
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• pp.235-245
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• 1989

The contents and the compositions of total free amino acids were investigated in the rice(Oryza sativa L. cv. Chuncheong) seedlings under low temperatures. Activities of some enzymes associated with the markedly changed amino acid content were also investigaetd. Under low temperature, the contents of soluble protein and the total free amino acids increased, while the content of total nitrogen decreased. Although asparagine＋glycine were the most abundant amino acid speceis in the rice seedlings at the control temeprature, low temperature treatment for 3days brought about the decrease in their amount to about 60% level of the control plants. On the other hand, alanine showed the highest increase in the content among all the free amino acids, though glutamine, proline, asprtic acid, valine and tyrosine also increased after low temperature treatment. To eludicate the decrease of asparagine＋glycine level under low temperature, the activities of asparagine aminotransferase and asparaginase which metabolize asparagine were investigated in the rice seedlings under low temperature. The activity of asparaginase increased markedly, while that of asparagine aminotransferase decreased under low temperatures. Therefore, it was suggested that asparaginase metabolizes asparagine predominatly in the rice seedlings under low temperatures.

• Food Science and Biotechnology
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• v.15 no.2
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• pp.177-182
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• 2006

Polyphenol oxidase (PPO) was isolated from the flesh of Fuji apples by DEAE-Cellulose, ammonium sulfate precipitation, phenyl-Sepharose CL-4B, and Sephdex G-100 chromatography. The molecular mass of the purified PPO was estimated to be 40 kDa by SDS polyacrylamide gel electrophoresis. With regard to substrate specificity, maximum activity was achieved with chlorogenic acid as substrate, followed by catechin and catechol whereas, there was no detectable activity with hydroquinic acid, resorcinol, or tyrosine as substrate. The optimum pH and temperature with catechol as substrate were 6.5 and $35^{\circ}C$, respectively. The enzyme was most stable at pH 6.0 and unstable at acidic pH. The enzyme was stable when it was heated to $45^{\circ}C$ but heating at $50^{\circ}C$ for more than 30 min caused 50% loss of activity. Reduced $ZnSO_4$, L-cystein, epigallocatechin-3-o-gallate (EGCG), and gallocatechin gallate (GCG) also inhibited activity.

• Korean Journal of Plant Resources
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• v.14 no.1
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• pp.32-37
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• 2001

Mammalian tyrosinase plays an important role in the process of melanin polymer biosynthesis by catalyzing the hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine(DOPA) and the oxidation of DOPA to dopaquinone. These processes are major determinant of human skin color and involved in localized hyperpigmentation. Therefore, the enzyme inhibitors have been of great concern as skin-whitening cosmetics. Methanol extracts of 174 oriental herbs were screened for the mushroom tyrosinase inhibitory activity.

• Fisheries and Aquatic Sciences
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• v.3 no.3_4
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• pp.188-194
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• 2000

A protease purified from hepatopancreas of shrimp, Penaeus japonicus, had maximum activity at $70^{\circ}C$ and in neutral and alkaline pH ranges. Specific activity at optimum reaction condition of the protease was estimated to be approximately 12 U/mg/min. The protease was stable in neutral and alkaline pH ranges and activity was retained after heat treatment at $50^{\circ}C$ for 30 min. Apparent $K_m$ and $V_{max}$ value against casein substrate were estimated to be $0.29\%$ and $7.8see^{-1}$, respectively, and those against N-CBZ-L-tyrosine p-nitropheny1 ester (CBZ­Tyr-NE) were 0.38 mM and $2,400 see^{-1}$, respectively. The N-termina1 sequence of the protease showed high homology to the trypsin from same species and the proteases from shrimp. Myosin heavy chain (MHC) from shrimp tail meat was the most susceptible to the protease and actin/tropomyosin were degraded progressively during 4 hr incubation, but to a lesser degree than MHC.

• Journal of the Korean Magnetic Resonance Society
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• v.4 no.2
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• pp.133-139
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• 2000

The strategy to incorporate [$^{15}$ N]-labeled amino acids were discussed. Instead of using specific auxotrophic strains for selective labeling, the prototrophic strain, BL2l(DE3), was used with a plasmid, pLysS, and found to be very effective for several amino acids including alanine, lysine, leucine, and threonine. Isoleucine, valine, glutamine, and tyrosine were also found to be effective despite some diffusion into other amino acids. Interesting result was obtained when [$^{15}$ N]-labeled glycine was tried: only glycines were labeled when amino acid mixture was added in the growth medium, and serines were co-labeled when amino acids were omitted. These results can be used as a guideline when selective labeling strategy is considered, and when the resulting data are interpreted.

• Natural Product Sciences
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• v.11 no.2
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• pp.89-91
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• 2005

Effect of the neolignans, honokiol (1) and magnolol (2), isolated from Magnoliae Cortex on mushroom tyrosinase activity was investigated in vitro using L-tyrosine as a substrate. Honokiol (1) inhibited tyrosinase activity significantly in a concentration-dependent manner, on the other hand, magnolol (2) did not show tyrosinase inhibitory effect. Honokiol exhibited tyrosinase inhibitory effect with $IC_{50}$ value of $67.9\;{\mu}M$, and proved to act as a non-competitive inhibitor by the analysis of Lineweaver-Burk plot.

• Bulletin of the Korean Chemical Society
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• v.31 no.4
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• pp.971-975
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• 2010

Eight hydroxylated stilbene derivatives including resveratrol, desoxyrhapontigenin and piceatannol as potential radical scavenger and tyrosinase inhibitor are synthesized using optimized Wittig-Horner reaction for excellent trans-selectivity in good yields. Antioxidant activity was tested against ABTS radical and tyrosinase inhibitory activity was performed with L-tyrosine as the substrate based on previous procedure with some modification. In general, catecholic stilbenes showed stronger activity against ABTS radical and resorcinolic moiety showed stronger tyrosinase inhibitory activity. Synthetic piceatannol which containing both catecholic and resorcinolic moieties showed the strongest activity in both as ABTS radical scavenger and tyrosinase inhibitor with $IC_{50}$ values of 4.1 and $8.6\;{\mu}M$, respectively.

• Korean Journal of Korean Medical Institute of Dermatology and Aesthetics
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• v.1 no.1
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• pp.5-15
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• 2005

The purpose of this study was to investigate the effect of the aqueous extract of the Astragalus membranaceous(AM). AM showed inhibitory effect on the tyrosinase activity using L-tyrosine as a substrate. Tyrosinase plays an important role in the process of melanin polymer biosynthesis. In vitro AM extract(1mg/ml) inhibited melanin biosynthesis and are useful for the material used in cosmetics. B16 mouse melanoma cells were cultured in different concentrations. The non-cytotoxicity of the plant extracts was confirmed by MTT assay.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.169.2-170
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• 2003

Erythropietin (EPO), a hematopoietic factor is also required for normal brain development, and its receptor is localized in brain. Therefore, it is possible that EPO could act as a neurotropic factor inducing differentiation of neurons. The present study, we therefore investigated whether EPO can increase differentiation of undifferentiated cortical neuron isolated from postneonatal (Day 1) rat brains and PC12 cell, undifferentiated dopaminagic cell line. EPO dose (1-100 U/ml) dependently increased cell differentiation and expression of differentiation marker gene (neurofilament and tyrosine hydroxylase) in both cells. (omitted)

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.79.3-80
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• 2003

The effects of anonaine, an aporphine isoquinoline alkaloid, on dopamine biosynthesis and L-DOPA-induced neurotoxicity in PC12 cells were investigated. Treatment of PC12 cells with 0.05 ${\mu}$M anonaine showed a significant inhibition of dopamine content. The IC$\sub$50/ value of anonaine was 0.05 ${\mu}$M. Under the same conditions, 0.05 ${\mu}$M anonaine also inhibited tyrosine hydroxylase (TH) activity at 24 h (62.0% inhibition of the control level). TH mRNA levels were also decreased by the treatment with anonaine. (omitted)