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Purification and Some Biological Properties of Asparaginase from Azotobacter vinelandii.

Applied and environmental microbiology

Gaffar SA, Shethna YI.
PMID: 16345199
Appl Environ Microbiol. 1977 Mar;33(3):508-14. doi: 10.1128/aem.33.3.508-514.1977.

Asparaginase was found in the soluble fraction of cells of Azotobacter vinelandii, and its activity remained the same during growth of the organism in a nitrogen-free medium. The specific activity and the yield of A. vinelandii increased twofold in...

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Gaffar SA, Shethna YI. Purification and Some Biological Properties of Asparaginase from Azotobacter vinelandii. Appl Environ Microbiol. 1977;33(3):508-14doi: 10.1128/aem.33.3.508-514.1977.
Gaffar, S. A., & Shethna, Y. I. (1977). Purification and Some Biological Properties of Asparaginase from Azotobacter vinelandii. Applied and environmental microbiology, 33(3), 508-14. https://doi.org/10.1128/aem.33.3.508-514.1977
Gaffar, S A, and Shethna, Y I. "Purification and Some Biological Properties of Asparaginase from Azotobacter vinelandii." Applied and environmental microbiology vol. 33,3 (1977): 508-14. doi: https://doi.org/10.1128/aem.33.3.508-514.1977
Gaffar SA, Shethna YI. Purification and Some Biological Properties of Asparaginase from Azotobacter vinelandii. Appl Environ Microbiol. 1977 Mar;33(3):508-14. doi: 10.1128/aem.33.3.508-514.1977. PMID: 16345199; PMCID: PMC170717.
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Regulation by sulfhydryl groups of glyceollin accumulation in soybean hypocotyls.

Planta

Stössel P.
PMID: 24258580
Planta. 1984 Mar;160(4):314-9. doi: 10.1007/BF00393412.

Hypocotyls of 5-d-old etiolated soybean seedlings (Glycine max (L.) Merr. cv. Altona) were treated with (a) dithiothreitol (DTT) or one of the sulfhydryl-binding reagents N-ethylmaleimide (NEM), p-hydroxymercuribenzoate (PMB) und p-chloromercuribenzene sulfonic acid (PMBS), (b) one of the sulfhydryl reagents...

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Stössel P. Regulation by sulfhydryl groups of glyceollin accumulation in soybean hypocotyls. Planta. 1984;160(4):314-9doi: 10.1007/BF00393412.
Stössel, P. (1984). Regulation by sulfhydryl groups of glyceollin accumulation in soybean hypocotyls. Planta, 160(4), 314-9. https://doi.org/10.1007/BF00393412
Stössel, P. "Regulation by sulfhydryl groups of glyceollin accumulation in soybean hypocotyls." Planta vol. 160,4 (1984): 314-9. doi: https://doi.org/10.1007/BF00393412
Stössel P. Regulation by sulfhydryl groups of glyceollin accumulation in soybean hypocotyls. Planta. 1984 Mar;160(4):314-9. doi: 10.1007/BF00393412. PMID: 24258580.
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Control of NADH ferricyanide reductase activity in the human erythrocyte by somatotrophin and insulin.

Redox report : communications in free radical research

Marques F, Crespo ME, Bicho M.
PMID: 27405553
Redox Rep. 1995 Feb;1(2):113-7. doi: 10.1080/13510002.1995.11746968.

Reduction of external ferricyanide by the human erythrocyte is significantly stimulated by insulin and somatotrophin at concentrations above physiological levels. Basal (in absence of hormones) and hormone-stimulated activities are attenuated in the presence of glycolytic inhibitors iodoacetate and vanadate...

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Marques F, Crespo ME, Bicho M. Control of NADH ferricyanide reductase activity in the human erythrocyte by somatotrophin and insulin. Redox Rep. 1995;1(2):113-7doi: 10.1080/13510002.1995.11746968.
Marques, F., Crespo, M. E., & Bicho, M. (1995). Control of NADH ferricyanide reductase activity in the human erythrocyte by somatotrophin and insulin. Redox report : communications in free radical research, 1(2), 113-7. https://doi.org/10.1080/13510002.1995.11746968
Marques, F, et al. "Control of NADH ferricyanide reductase activity in the human erythrocyte by somatotrophin and insulin." Redox report : communications in free radical research vol. 1,2 (1995): 113-7. doi: https://doi.org/10.1080/13510002.1995.11746968
Marques F, Crespo ME, Bicho M. Control of NADH ferricyanide reductase activity in the human erythrocyte by somatotrophin and insulin. Redox Rep. 1995 Feb;1(2):113-7. doi: 10.1080/13510002.1995.11746968. PMID: 27405553.
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Induction of Rishitin and Lubimin Synthesis in Potato Tuber Slices by Non-Specific Elicitors - Role of Gene Derepression.

Journal of food protection

Cheema AS, Haard NF.
PMID: 30812259
J Food Prot. 1979 Jun;42(6):512-518. doi: 10.4315/0362-028X-42.6.512.

The stress metabolites rishitin and lubimin accumulate at relatively low concentrations (5-20 ppm) in potato tuber slices subjected to various cell-disruptive treatments including heavy metal salts, sulfhydryl reagents, metabolic inhibitors, detergents, ultraviolet light and lysosomal enzymes. Cold-stored (4 C)...

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Cheema AS, Haard NF. Induction of Rishitin and Lubimin Synthesis in Potato Tuber Slices by Non-Specific Elicitors - Role of Gene Derepression. J Food Prot. 1979;42(6):512-518doi: 10.4315/0362-028X-42.6.512.
Cheema, A. S., & Haard, N. F. (1979). Induction of Rishitin and Lubimin Synthesis in Potato Tuber Slices by Non-Specific Elicitors - Role of Gene Derepression. Journal of food protection, 42(6), 512-518. https://doi.org/10.4315/0362-028X-42.6.512
Cheema, A S, and Haard, N F. "Induction of Rishitin and Lubimin Synthesis in Potato Tuber Slices by Non-Specific Elicitors - Role of Gene Derepression." Journal of food protection vol. 42,6 (1979): 512-518. doi: https://doi.org/10.4315/0362-028X-42.6.512
Cheema AS, Haard NF. Induction of Rishitin and Lubimin Synthesis in Potato Tuber Slices by Non-Specific Elicitors - Role of Gene Derepression. J Food Prot. 1979 Jun;42(6):512-518. doi: 10.4315/0362-028X-42.6.512. PMID: 30812259.
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Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes*.

Enzyme and microbial technology

Yang J, Shih I, Tzeng Y, Wang S.
PMID: 10713215
Enzyme Microb Technol. 2000 Mar 01;26(5):406-413. doi: 10.1016/s0141-0229(99)00164-7.

A protease-producing microorganism was isolated in northern Taiwan and identified as a strain of Bacillus subtilis. B. subtilis Y-108 thus isolated can be used for deproteinization of crustacean wastes in the preparation of chitin. For deproteinization tests, liquid phase...

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Yang J, Shih I, Tzeng Y, et al. Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes*. Enzyme Microb Technol. 2000;26(5):406-413doi: 10.1016/s0141-0229(99)00164-7.
Yang, J., Shih, I., Tzeng, Y., & Wang, S. (2000). Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes*. Enzyme and microbial technology, 26(5), 406-413. https://doi.org/10.1016/s0141-0229(99)00164-7
Yang, et al. "Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes*." Enzyme and microbial technology vol. 26,5 (2000): 406-413. doi: https://doi.org/10.1016/s0141-0229(99)00164-7
Yang J, Shih I, Tzeng Y, Wang S. Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes*. Enzyme Microb Technol. 2000 Mar 01;26(5):406-413. doi: 10.1016/s0141-0229(99)00164-7. PMID: 10713215.
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Covalent and Noncovalent Dimers of the Cyanide-Resistant Alternative Oxidase Protein in Higher Plant Mitochondria and Their Relationship to Enzyme Activity.

Plant physiology

Umbach AL, Siedow JN.
PMID: 12231983
Plant Physiol. 1993 Nov;103(3):845-854. doi: 10.1104/pp.103.3.845.

Evidence for a mixed population of covalently and noncovalently associated dimers of the cyanide-resistant alternative oxidase protein in plant mitochondria is presented. High molecular mass (oxidized) species of the alternative oxidase protein, having masses predicted for homodimers, appeared on...

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Umbach AL, Siedow JN. Covalent and Noncovalent Dimers of the Cyanide-Resistant Alternative Oxidase Protein in Higher Plant Mitochondria and Their Relationship to Enzyme Activity. Plant Physiol. 1993;103(3):845-854doi: 10.1104/pp.103.3.845.
Umbach, A. L., & Siedow, J. N. (1993). Covalent and Noncovalent Dimers of the Cyanide-Resistant Alternative Oxidase Protein in Higher Plant Mitochondria and Their Relationship to Enzyme Activity. Plant physiology, 103(3), 845-854. https://doi.org/10.1104/pp.103.3.845
Umbach, A. L., and Siedow, J. N.. "Covalent and Noncovalent Dimers of the Cyanide-Resistant Alternative Oxidase Protein in Higher Plant Mitochondria and Their Relationship to Enzyme Activity." Plant physiology vol. 103,3 (1993): 845-854. doi: https://doi.org/10.1104/pp.103.3.845
Umbach AL, Siedow JN. Covalent and Noncovalent Dimers of the Cyanide-Resistant Alternative Oxidase Protein in Higher Plant Mitochondria and Their Relationship to Enzyme Activity. Plant Physiol. 1993 Nov;103(3):845-854. doi: 10.1104/pp.103.3.845. PMID: 12231983; PMCID: PMC159055.
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Hemoglobin-digesting Acid Proteinases in Soybean Leaves: CHARACTERISTICS AND CHANGES DURING LEAF MATURATION AND SENESCENCE.

Plant physiology

Ragster LV, Chrispeels MJ.
PMID: 16661607
Plant Physiol. 1981 Jan;67(1):110-4. doi: 10.1104/pp.67.1.110.

Three proteinases which digest hemoglobin rapidly at acid pH (3.5 to 4.5) were identified in crude extracts of soybean (Merr.) leaves and separated by chromatography on DEAE-cellulose. All three enzymes were endopeptidases as judged by the ratio of alpha-amino-nitrogen...

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Ragster LV, Chrispeels MJ. Hemoglobin-digesting Acid Proteinases in Soybean Leaves: CHARACTERISTICS AND CHANGES DURING LEAF MATURATION AND SENESCENCE. Plant Physiol. 1981;67(1):110-4doi: 10.1104/pp.67.1.110.
Ragster, L. V., & Chrispeels, M. J. (1981). Hemoglobin-digesting Acid Proteinases in Soybean Leaves: CHARACTERISTICS AND CHANGES DURING LEAF MATURATION AND SENESCENCE. Plant physiology, 67(1), 110-4. https://doi.org/10.1104/pp.67.1.110
Ragster, L V, and Chrispeels, M J. "Hemoglobin-digesting Acid Proteinases in Soybean Leaves: CHARACTERISTICS AND CHANGES DURING LEAF MATURATION AND SENESCENCE." Plant physiology vol. 67,1 (1981): 110-4. doi: https://doi.org/10.1104/pp.67.1.110
Ragster LV, Chrispeels MJ. Hemoglobin-digesting Acid Proteinases in Soybean Leaves: CHARACTERISTICS AND CHANGES DURING LEAF MATURATION AND SENESCENCE. Plant Physiol. 1981 Jan;67(1):110-4. doi: 10.1104/pp.67.1.110. PMID: 16661607; PMCID: PMC425631.
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Leaf Proteolytic Activities and Senescence during Grain Development of Field-grown Corn (Zea mays L.).

Plant physiology

Feller UK, Soong TS, Hageman RH.
PMID: 16659836
Plant Physiol. 1977 Feb;59(2):290-4. doi: 10.1104/pp.59.2.290.

Some proteolytic enzymes occurring in the leaves of field-grown corn (Zea mays) (B73) were identified and partially characterized. Changes in activities of several proteolytic enzymes and in concentrations of protein and chlorophyll as a function of intraleaf segments (tip...

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Feller UK, Soong TS, Hageman RH. Leaf Proteolytic Activities and Senescence during Grain Development of Field-grown Corn (Zea mays L.). Plant Physiol. 1977;59(2):290-4doi: 10.1104/pp.59.2.290.
Feller, U. K., Soong, T. S., & Hageman, R. H. (1977). Leaf Proteolytic Activities and Senescence during Grain Development of Field-grown Corn (Zea mays L.). Plant physiology, 59(2), 290-4. https://doi.org/10.1104/pp.59.2.290
Feller, U K, et al. "Leaf Proteolytic Activities and Senescence during Grain Development of Field-grown Corn (Zea mays L.)." Plant physiology vol. 59,2 (1977): 290-4. doi: https://doi.org/10.1104/pp.59.2.290
Feller UK, Soong TS, Hageman RH. Leaf Proteolytic Activities and Senescence during Grain Development of Field-grown Corn (Zea mays L.). Plant Physiol. 1977 Feb;59(2):290-4. doi: 10.1104/pp.59.2.290. PMID: 16659836; PMCID: PMC542384.
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Sulfhydryl Group Involvement in Plasmalemma Transport of HCO(3) and OH in Chara corallina.

Plant physiology

Lucas WJ, Alexander JM.
PMID: 16661173
Plant Physiol. 1980 Feb;65(2):274-80. doi: 10.1104/pp.65.2.274.

The effect of the sulfhydryl reagents (-SH) p-chloromercuribenzene-sulfonic acid (PCMBS), N-ethylmaleimide (NEM), and inorganic mercury on H(14)CO(3) (-) assimilation in Chara corallina is reported. Commercial grade PCMBS caused severe inhibition of H(14)CO(3) (-) assimilation. Results obtained using purified PCMBS...

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Lucas WJ, Alexander JM. Sulfhydryl Group Involvement in Plasmalemma Transport of HCO(3) and OH in Chara corallina. Plant Physiol. 1980;65(2):274-80doi: 10.1104/pp.65.2.274.
Lucas, W. J., & Alexander, J. M. (1980). Sulfhydryl Group Involvement in Plasmalemma Transport of HCO(3) and OH in Chara corallina. Plant physiology, 65(2), 274-80. https://doi.org/10.1104/pp.65.2.274
Lucas, W J, and Alexander, J M. "Sulfhydryl Group Involvement in Plasmalemma Transport of HCO(3) and OH in Chara corallina." Plant physiology vol. 65,2 (1980): 274-80. doi: https://doi.org/10.1104/pp.65.2.274
Lucas WJ, Alexander JM. Sulfhydryl Group Involvement in Plasmalemma Transport of HCO(3) and OH in Chara corallina. Plant Physiol. 1980 Feb;65(2):274-80. doi: 10.1104/pp.65.2.274. PMID: 16661173; PMCID: PMC440310.
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Asparagine synthesis in pea leaves, and the occurrence of an asparagine synthetase inhibitor.

Plant physiology

Joy KW, Ireland RJ, Lea PJ.
PMID: 16663168
Plant Physiol. 1983 Sep;73(1):165-8. doi: 10.1104/pp.73.1.165.

Asparagine is present in the mature leaves of young pea (Pisum sativum cv Little Marvel) seedlings, and is synthesized in detached shoots. This accumulation and synthesis is greatly enhanced by darkening. In detached control shoots, [(14)C]aspartate was metabolized predominantly...

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Joy KW, Ireland RJ, Lea PJ. Asparagine synthesis in pea leaves, and the occurrence of an asparagine synthetase inhibitor. Plant Physiol. 1983;73(1):165-8doi: 10.1104/pp.73.1.165.
Joy, K. W., Ireland, R. J., & Lea, P. J. (1983). Asparagine synthesis in pea leaves, and the occurrence of an asparagine synthetase inhibitor. Plant physiology, 73(1), 165-8. https://doi.org/10.1104/pp.73.1.165
Joy, K W, et al. "Asparagine synthesis in pea leaves, and the occurrence of an asparagine synthetase inhibitor." Plant physiology vol. 73,1 (1983): 165-8. doi: https://doi.org/10.1104/pp.73.1.165
Joy KW, Ireland RJ, Lea PJ. Asparagine synthesis in pea leaves, and the occurrence of an asparagine synthetase inhibitor. Plant Physiol. 1983 Sep;73(1):165-8. doi: 10.1104/pp.73.1.165. PMID: 16663168; PMCID: PMC1066427.
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The respiratory burst and electrolyte leakage induced by sulfhydryl blockers in egeria densa leaves are associated with H2O2 production and are dependent on Ca2+ influx .

Plant physiology

Albergoni F, Amicucci E, Marre MT, Marre E, Zingarelli L.
PMID: 9847112
Plant Physiol. 1998 Dec;118(4):1379-87. doi: 10.1104/pp.118.4.1379.
Free PMC Article

In leaves of Egeria densa Planchon, N-ethylmaleimide (NEM) and other sulfhydryl-binding reagents induce a temporary increase in nonmitochondrial respiration (DeltaQO2) that is inhibited by diphenylene iodonium and quinacrine, two known inhibitors of the plasma membrane NADPH oxidase, and are...

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Albergoni F, Amicucci E, Marre MT, et al. The respiratory burst and electrolyte leakage induced by sulfhydryl blockers in egeria densa leaves are associated with H2O2 production and are dependent on Ca2+ influx . Plant Physiol. 1998;118(4):1379-87doi: 10.1104/pp.118.4.1379.
Albergoni, F., Amicucci, E., Marre, M. T., Marre, E., & Zingarelli, L. (1998). The respiratory burst and electrolyte leakage induced by sulfhydryl blockers in egeria densa leaves are associated with H2O2 production and are dependent on Ca2+ influx . Plant physiology, 118(4), 1379-87. https://doi.org/10.1104/pp.118.4.1379
Albergoni, et al. "The respiratory burst and electrolyte leakage induced by sulfhydryl blockers in egeria densa leaves are associated with H2O2 production and are dependent on Ca2+ influx ." Plant physiology vol. 118,4 (1998): 1379-87. doi: https://doi.org/10.1104/pp.118.4.1379
Albergoni F, Amicucci E, Marre MT, Marre E, Zingarelli L. The respiratory burst and electrolyte leakage induced by sulfhydryl blockers in egeria densa leaves are associated with H2O2 production and are dependent on Ca2+ influx . Plant Physiol. 1998 Dec;118(4):1379-87. doi: 10.1104/pp.118.4.1379. PMID: 9847112; PMCID: PMC34754.
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Showing 49 to 59 of 59 entries