• The Korean Journal of Zoology
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• v.16 no.1
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• pp.67-77
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• 1973

The alcohol dehydrogenase (ADH) isozyme of the four strains of Drosophila melanogaster in Korea was studied by the starch gel electrophoresis and the results are given below: 1. The numbers of bands, staining intensity and mobility are considerably variable in the three strains, Chunchun, Jinju and Sinchon-Seoul, but relatively uniform in the Taijun strain. 2. It is suggested that the Taijun strain may be homogeneous and the other three strains, on the contrary, heterogeneous for the ADH constitution. 3. The electrophoretic patterns are observed to be different between males and females in all strains used which is hard to intereret. 4. The starch gel electrophoresis is to have a resolving power superior to cellulose acetate electrophoresis.

• International Journal of Industrial Entomology and Biomaterials
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• v.14 no.1
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• pp.37-44
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• 2007

A study was made of the haemolymph protein spectrum of mulberry silkworm (Bomhyx mori L.) from the first larval instar to imago. Horizontal starch gel electrophoresis was used. Sixteen races and eight F1 interracial hybrids, raised in Bulgaria, were analyzed. During the ontogenesis, a total of 17 protein bands (15 cathodic and 2 anodic) were detected. Distinct dynamics in the haemolymph protein spectrum was observed, in result of different expression during the individual development associated with the processes of growth, histolysis and histogenesis. Based on the ontogenetic dynamics found, a correspondence was assumed between some proteins detected by us using the starch gel electrophoresis and major haemolymph proteins (SP1, SP2, MHPs and Vg) detected by other authors using the polyacrilamide gel electrophoresis. Intraracial and interracial polymorphism was observed in four protein zones. The effect of four polymorphic loci with codominant and null alleles was suggested.

• Microbiology and Biotechnology Letters
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• v.9 no.4
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• pp.185-190
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• 1981

1. $\alpha$-amylase from B. circulans F-2 was purified with specific activity 55.0 u/mg. protein (about 23 times of the original specific activity) and the yield of 25.5%, by means of corn starch absorption, salting out with ammonium sulfate (80% saturation), gel filtration on Bio-Gel P-100 and DE-32 column chromatography. 2 The purified enzyme showed two closely migrated protin bands on polyacrylamide disc gel electrophoresis, both of which have amylase activity judging from the activity staining of the gel. On SDS-polyacrylamide disc gel electrophoresis, however, the purified enzyme showed a single band suggesting that those two bands are the charge isomers of an amlyase having the slightly different charge. 3. Plot of log mobility of two bands versus polyacrylamide gel concentration according to Hedrick and Smith gave the parallel lines indicating them to be charge isomers. 4. To confirm the action pattern of two enzyme protein bands, each band was separated and was eluted from the gel and eluates were incubated with soluble starch. Oligosaccharide pattern produced by each eluate was examined by paper chromatography. The eluates of two bands showed the same action pattern. 5. The maltohexaose was the only hydrolysis product of soluble starch in the early stage of hydrolysis.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.30 no.4
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• pp.405-411
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• 1985

The buffer soluble proteins were extracted from six cultivars of barley grains and analyzed by various electrophoresis; 7.5% polyacrylamide slab gel, 2-30% polyacrylamide porosity gradient tube gel, isoelectric focusing (pH4-9) and starch gel electrophoresis. The proteins, esterase, acid phosphatase, malate dehydrogenase, glutamate dehydrogenase and leucine aminopeptidase were investigated to find out the best method to differentiate barley cultivars. The result were that protein and esterase bands in 2-30% polyacrylamide porosity gradient tube gel electrophoresis and protein bands in 7.5% polyacrylamide slab gel electrophoresis showed typical varietal differences. Therefore, those methods were suitable for differentiation of barley cultivars. It was difficult to differentiate the cultivars by the other methodes and patterns of the other enzymes.

• Korean Journal of Food Science and Technology
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• v.18 no.4
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• pp.288-293
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• 1986

A raw starch-digesting enzyme from Rhizopus oryzae was purified by ammonium sulfate fractionation, DEAE-sephacel column chromatography and Sephadex G-150 gel filtration. The specific activity of purified enzyme was 45.2 Ulmg protein and the yield was 16.2%. The purified enzyme was found to be homogeneous bypolyacrylamide gel electrophoresis and its molecular weight was estimated to be 67,000 by SDS-polyacrylamide gel electrophoresis, and also the enzyme had Km value of 4.082 mg/ml for raw corn starch. The optimal temperature and pH for the enzyme activity were $50^{\circ}C$ and 4.0-5.0, respectively. Reaction product of raw corn starch by purified enzyme was glucose mainly.

• Korean Journal of Veterinary Research
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• v.24 no.1
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• pp.31-35
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• 1984

The hemoglobin phenotype and the gene frequencies of 44 Formosan deer(Cervus nippon) in Kyung-Gi area were examined by using cellulose acetate and starch gel electrophoresis. 1. The method of cellulose acetate electrophoresis was simplier, more clear and preserative than starch gel electrophoresis. 2. The hemoglobin phenotype was appeared 3 types as $Hb^F$ $Hb^{FS}$ and $Hb^S$. The frequencies of appearance were $Hb^F$ 47.7%, $Hb^{FS}$ 47.7% and $Hb^S$ 4.5%, respectively. 3. The genetic factors of hemoglobin were observed as $Hb^F$ and $Hb^S$ and the rates of gene frequencies were 71.6% and 28.4%, respectively.

• Korean Journal of Veterinary Research
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• v.15 no.1
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• pp.19-22
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• 1975

The serum albumin phenotypes and the gene frquencies of 100 Korean native goats were examined by starch gel electrohporesis. The results obtained were as follows: 1. The albumin phenotypes were classified as Alb AA, Alb AB, and Alb BB and the frequencies of appearence were 10, 12 and 78%, respectively. 2. The genetic factors of serum albumin were observed as Alb A and Alb B and the rates of gene frequencies were 16 and 84%, respectively.

• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.136-141
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• 1989

A raw starch-digesting enzyme from Streptomyces sp. 4M-2 was purified by ammonium sulfate fractionation, DEAE-Sephadex A-50 column chromatography and Sephadex G-100 gel filtration. The specific activity of the purified enzyme was 51.22 RSU/mg protein and the yield was 4.5% of the total activity of the culture broth. The purified enzyme was found to be homogeneous by polyacrylamide gel electrophoresis and its molecular weight was estimated to be about 102, 000 daltons by SDS-polyacrylamide gel electrophoresis, The optimal temperature and pH for the enzyme activity were 42$^{\circ}C$ and PH 5.5, respectively. The enzyme had Km, value of 44.44mg/$m\ell$ for raw corn starch. The enzyme was activated by addition of calcium and barium ions. Corn amylose was degraded by the enzyme very easily and raw potato starch was also degraded easily. Main products of the enzymatic hydrolysis of raw corn starch were analyzed to be maltose and maltotriose. The enzyme was considered as $\alpha$-amylase.

• Asian-Australasian Journal of Animal Sciences
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• v.8 no.4
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• pp.353-356
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• 1995

The red cell X-protein, NADH-diaphorase 1, malic enzyme and serum arylesterase phenotypes of 50 Thai Longtail and 53 Cameroon X Thai Longtail ($F_1$) crossbred sheep were determined by horizontal starch gel electrophoresis. None of the economic traits was influenced by DIA1, ME and EsA phenotypes. However, XP phenotypes showed a highly significant association with body weight, body height, heart girth and back girth, with mean values of XP+ve phenotype greater than XP-ve. The $XP^+$ allele was associated with greater body weight, body height, heart girth and back girth.

• Microbiology and Biotechnology Letters
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• v.25 no.2
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• pp.166-172
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• 1997

Aspergillus niger was selected as a strain producing the potent raw starch hydorlyzing enzyme. These experiments were conducted to investigate the conditions of the glucoa- mylase production, the purification of the enzyme, some characteristics of the purified enzyme and hydrolysis rate on various raw starches such as com, rice, potato, glutinous rice, sweet potato, wheat and barley. The optimum cultural temperature and time for the enzyme production on wheat bran medium were $30^{\circ}C$ and 96hrs, respectively. The respective addition of yeast extract and nutrient broth on wheat bran medium increased slightly the enzyme production. The enzyme was purified by ammonium sulfate fractionation and DEAE-cellulose column chromatography. The specific activity of the purified enzyme was 30.7u/mg-protein and the yield of enzyme activity was 25.8%. The purified enzyme showed a single band on polyacrylamide disc gel electrophoresis and its molecular weight was estimated to be 56,000 by SDS-polyacrylamide disc gel electrophoresis. The isoelectric point for the purified enzyme was pH3.7. The optimum temperature and pH were $65^{\circ}C$ and pH 4.0, respectively. The purified enzyme was stable in the pH range of pH 3.0-9.5 and below $45^{\circ}C$, and its thermal stability was slightly increased by the addition of $Ca^{2+}$. The purified enzyme was activated by $Co^{2+},\;Sr^{2+},\;Mn^{2+},\;Fe^{2+},\;Cu^{2+}$. Raw rice starch, raw corn starch, raw glutinous rice starch, raw sweet potato starch, raw wheat starch and raw barley starch showed more than 90% hydrolysis rate in 48hrs incubation. Even raw potato starch, most difficult to be hydrolyzed, showed 80% hydrolysis rate. The purified enzyme was identified as glucoamylase.