• Journal of Plant Biology
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• v.36 no.4
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• pp.307-312
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• 1993

In germinating pea, contents of enodgenous polyamine in the leaf and stem were determined, and protein content, peroxidase activity and pattern of isozymes were examined in the leaf treated with polyamines. During growth of the pea for 14 days in light condition, the polyamines in leaf and stem showed the highest level at the 5th day, and were decreased rapidly at the 7th day, kept almost constant level since then. The putrescine level was relatively higher than those of spermidine and spermine, and cadaverine was also detected. On the other hand, in the leaf treated with spermine (0.01 mM) protein content increased about 250% than that of the control, the peroxidase activity increased ore than 100% in spermine of 0.01 mM and 0.1 mM. In treating with putrescine of 0.1 mM the pattern of peroxidase isozyme appeared 4 new cathodic bands (pI 4.8, 5.6, 5.9 and 6.8) compared with the control, the clear cathodic bands (pI 5.6, 5.9, 6.4 and 6.6) were also observed in spermine of 0.1 mM. These results suggest that polyamines were important factor in the differentiation of pea at the early stage of germination.

• Journal of Plant Biotechnology
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• v.4 no.1
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• pp.39-44
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• 2002

The fast-migrating cationic peroxidase isozyme, named RC3, was purified from rice (Oryza sativa cv. Nak-Dong) callus. Purification of the enzyme was accomplished by ammonium sulfate fractionation, CM-cellulose ionexchange chromatography, and Sephacryl S-100 gel filtration. The molecular mass of the enzyme was about 34 KDa as determined by SDS-PACE and 38 KDa by Sephacryl-100 gel filtration. The pI value of the enzyme was 8.9. Antiserum against RC3 was raised in rabbits, and anti RC3 antiserum reacted with RC3 isozyme by Ouchterlony double immunodiffusion. The optimum pHs and Km values of the enzyme for various substrates were determined. Kinetic studies with various substrates showed that RC3 had very low Km value of 0.01 mM for ferulic acid and ascorbic acid. However, the enzyme did not use esculetin as a substrate.

• The Korean Journal of Mycology
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• v.16 no.2
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• pp.87-94
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• 1988

Electrophoretic isozyme patterns from mycelia, primordia, cap and stem of Pleurotus spp. collected in Korea were compared. Primordia, cap and stem of fruitbody showed very similar isozyme patterns but mycelial isozyme patterns were different from those of fruitbody. Isozyme patterns of malate dehydrogenase, acid phosphatase in Pleurotus ostreatus collected from different regions in Korea were similar but those of esterase, peroxidase, leucine amino peptidase and superoxide dismutase were different. Interspecific comparison of esterase isozyme patterns among Pleurotus ostreatus P. cornucopiae and, P. florida was very different and may be valuable subsidiary tool to conventional taxonomic techniques for identifying species of Pleurotus. A dendrogram by similarities of isozyme band pattern was presented.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.29 no.1
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• pp.39-45
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• 1984

The present researches were carried out to investigate the effects of gibberellic acid on the appearance of isozyme patterns of esterase, phosphatase, amylase and peroxidase, also to investigate if there were any differences of the isozyme patterns among root, shoot and seeds of rice plants. It was noticed that the isozyme patterns of the above tested enzymes were differ among the organs, root, shoot and seed. The GA treated plants showed difference of esterase patterns in root from Akibare and the difference in shoot and root from Yushin, phosphatase patterns in root from Akibare. However, the GA did not affect isozyme patterns of amylase or peroxidase. The seed should be the suitable organ to study isozyme patterns for genetics or variety characterization of rice plant.

• The Korean Journal of Ecology
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• v.21 no.6
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• pp.771-777
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• 1998

Aqueous extracts of Pinus rigida changed the electrophoretic patterns of total proteins and of hydrolytic enzymes such as peroxidase, esterase and amylase during the germination of radish (Raphanus sativus var. hortensis for. acanthiformis). When the extract treatment was finished, at the late stage of radish germination, aqueous extracts of P. rigida had suppressed the expression of 24 KD and 60 KD proteins. the extract induced new isozyme bands, indicating concomitant activity of peroxidases, esterase activities were stimulated in the cathodic region. The activity of amylase was enhanced by the extract.

• Korean Journal of Food Science and Technology
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• v.23 no.4
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• pp.442-446
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• 1991

Three peroxidase fractions (peak I, II, III) were isolated from Fuji apples using CM-cellulose chromatography. The homogeneity of the isolated peroxidase isozymes was established by isoelectric focusing and electrophoresis. Isoelectric points of the isozymes were 3.80, 3.82, and 3.85, respectively. The optimum pH of peroxidase isozymes were pH 5.0(peak I) or 5.5(peak II, III), and optimum temperature was $40^{\circ}C$ when assayed by using guaiacol and $H_{2}O_{2}$ as substrates. Inactivation rate of three peroxidase isozymes were different at temperature of $70^{\circ}C$ and at pH of 5.5. The isozyme of peak II was found to be more heat stable than those of peak I and III. D values at $70^{\circ}C$ of peroxidase isozymes (peak I, II, III) were estimated to be 660 sec, 1,320 sec, and 600 sec, respectively. The thermal stability of Fuji apple peroxidase was not influenced in the presence of 0.032 M sucrose or lactose. However, the thermal stability of the enzyme was decreased by fructose and glucose.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.34 no.3
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• pp.270-273
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• 1989

This study was carried out to know the physiological characteristics related to flooding tolerance of rice plants. Peroxidase specific activities and banding pattern of peroxidase isozyme of 24 days old seedlings were analyzed after 3 days of flooding treatment in the artificial flooding tank. Peroxidase activities of japonica rice varieties which were relatively susceptible to submergence were higher in comparison to those of Tongil and indica rice varieties. And a peculier band of peroxidase isozyme which was not shown in any part of rice plant if not flooded, was appeared at the around 9 of isoelectric point in the leaf blade of japonica rice varieties when flooded.

• Applied Biological Chemistry
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• v.29 no.3
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• pp.279-287
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• 1986

The changes in peroxidase activity and its isozyme pattern in the different parts of mung bean sprout were investigated; The enzyme activity in cotyledon and root showed a tendency to increase at an early stage and then decreased gradually as germination continued. However, the crude homogenate of epicotyl and hypocotyl showed a continuous decline in the enzyme activity. In particular, the enzyme activity of the root was $1.5{\sim}3.5$ times higher than that of other parts. Gel electrophoresis of the crude homogenate revealed that the number of isozyme in every part of the mung bean sprout increase during germination up to 6th days. Two isozymes from root were partially purified by ammonium sulfate fractionation, gel filtration by Sephadex G-75 and DEAE cellulose column chromatography. One of the isozymes (A) was purified 16-fold by the present procedure, but the purity of the other isosyme (B) was not increased , significantly. Isozyme A was the most active at $65^{\circ}C$ and isozyme B at $70^{\circ}C$, while both isozyme (A, B) have a optimal pH of 5.6. The Km values of isozyme A and B for 0-dianisidine as a hydrogen donor determined to be 0.071 mM and 0.052mM, respectively, and those for isozyme A and B using $H_2O_2$ as a hydrogen acceptor were 0.28mM and 0.23mM, respectively.

• Korean journal of applied entomology
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• v.21 no.1 s.50
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• pp.23-26
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• 1982

The present study was carried out to investigate the change of peroxidase activity of soybean seed infected with Cerrospora kikurhii. The protein content, polyphenol oxidase activity and peroxidase isozyme pattern in health and infected soybean seed were also compared. 1. The peroxidase activity was substantially higher in the infected soybean seeds than that in the healthy seeds either cracked or not. No significant differences in protein content were recognized among the seeds tested. 2. No significant differences in peroxidase activities and protein contents were notified between healthy and infected seeds from the measurements on each parts of dissected seeds, cotyledon and seedcoat, however the peroxidase activity in the seed coat of the stained seed was 2.5 times to healthy seed. 3. The activities of polyphenel oxidase were undectable in both healthy and diseased seeds. 4. The electrophoretic Patterns of the Peroridase isozyme were the same between healthy and in footed seed. 5. Therefore, the increase of peroxidase activity in infected soybean seedcoat was mainly due to the biochemical reaction against the pathogen.

• Applied Biological Chemistry
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• v.34 no.2
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• pp.134-141
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• 1991

In order to investigate the changes and characteristics of biochemical metabolic substances of soybean tissue culture during the cultural period, immature cotyledons were detached form the plant on 15th days after flowering and cultured in vitro for 3 weeks. The cultures were classified into embryogenic(EC) and non-embryogenic callus(NEC). A part of the EC lines were subcultured for another 3 weeks and classified into root forming(RFC), and shoot forming cultures(SFC). Another part of the EC lines were used for isolation of protoplasts, which were subsequently cultured in vitro for 4 weeks. The cultures were classified into embryogenic(PEC) and non-embryogenic callus(PNEC) derived from the protoplasts. The cultures of EC and PEC lines showed higher phenylalanine content and lower methionine content than those of NEC and PNEC. At organ differentiation stage, both cultures showed the content of aspartic acid decreased, while the other amino acids increased as a whole. The protein pattern analysis of the cultures revealed that EC and NEC lines contained distinctive polypeptides, with mass of ca. 18KD for EC and ca. 22KD for NEC respectively. The EC and PEC lines also showed high activity of peroxidase isozyme A(piA), while the RFC and SFC lines showed that of peroxidase isozyme B(piB).