Amylase, Alpha References

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• Babson, S., and Babson, A.: An Improved Amylase Assay Using Dyed Amylopectin , Clin Chim Acta 44, 193, 1973
• Bajpai, P., and Bajpai, P.: High-Temperature Alkaline alpha-Amylase from Bacillus licheniformis, Biotechnol Bioeng 33, 72, 1989
• Bajpai, P., Gera, R., and Bajpai, P.: Optimization Studies for the Production of alpha-Amylase Using Cheese Whey Medium, Enzyme Microb Technol 14, 679, 1992
• Ball, W.: Isolation of Salivary Ribonuclease, Deoxyribonuclease, and Amylase from the Parotid Gland of the Rat, Rattus norvegicius albinus , Biochim Biophys Acta 341, 305, 1974
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• Beers, E., Duke, S.: Characterization of Alpha-Amylase from Shoots and Cotyledons of Pea (Pisum-Sativum L) Seedlings, Plant Physiol 92, 1154, 1990
• Berk, J., Kawaguchi, M., Zeineh, R., Ujihira, I., and Searcy, R.: Chromatographic Heterogeneity of Rabbit Serum Amylase , Science 141, 1182, 1963
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• Bernfeld, P.: Amylases alpha and beta, Meth Enzymol 1, 149, 1955
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• Biely, P., Mislovicova, D., Markovic, O., and Kalac, V.: A New Chromogenic Substrate for Assay and Detection of alpha-Amylase , Anal Biochem 172, 176, 1988
• Boyer, E., and Ingle, M.: Extracellular Alkaline Amylase from a Bacillus Species , J Bacteriol 110, 992, 1972
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• Brena, B., Pazos, C., Franco-Fraguas, L., and Batista-Viera, F.: Chromatographic Methods for Amylases , J Chromatogr B Biomed Appl 684, 217, 1996
• Buisson, G., Duee, E., Haser, R., and Payan, F.: Three Dimensional Structure of Porcine Pancreatic alpha-Amylase at 2.9 Å Resolution. Role of Calcium in Structure and Activity , EMBO J 6, 3909, 1987
• Buonocore, V., Poerio, E., Gramenzi, F., and Silano, V.: Affinity Column Purification of Amylases on Protein Inhibitors from Wheat Kernel , J Chromatogr 114, 109, 1975
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• Carlsen, M., Nielsen, J., and Villadsen, J.: Growth and a-amylase by Aspergillus oryzae during Continuous Cultivations, J Biotechnol 45, 81, 1996
• Carter, J., Staples, W., and Sinson, E.: Interference with the Amyloclastic Determination of Serum Amylase , Clin Chem 19, 686, 1973
• Ceska, M.: A Comparative alpha-Amylase Study Using an Agar Medium , Clin Chim Acta 36, 419, 1972
• Chan, Y., Braun, P., French, D., and Robyt, J.: Porcine Pancreatic alpha-Amylase Hydrolysis of Hydroxyethylated Amylose and Specificity of Subsite Binding , Biochemistry 23, 5795, 1984
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• Chang, Q., and Chen, J.: Separation of a-Amylase by Reversed Micellar Extraction. Effect of Solvent Type and Cosolvent Concentration on the Transfer Process , Appl Biochem Biotechnol 62, 119, 1997
• Cozzone, P., Pasero, L., and Marchis-Mouren, G.: Characterization of Porcine Pancreatic Isoamylases: Separation and Amino Acid Composition , Biochim Biophys Acta 200, 590, 1970
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• Daussant, J., and Renard, M.: Immunochemical Comparisons of alpha-Amylases in Developing and Germinating Wheat Seeds , F.E.B.S. Lett. 22, 301, 1972
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• Dellweg, H., John, M., and Schmidt, J.: Amylases from Pseudomonas stutzeri. Affinity Chromatography of Exo-Maltotetrahydrolase Using Sephadex G-100 as an Adsorbent, Eur J Appl Microb 1, 191, 1975
• Dercova, K., Augustin, J., and Krajcova, D.: Cell Growth and alpha-Amylase Production Characteristics of Bacillus subtilis , Folia Microbiol (Praha) 37, 17, 1992
• El-Baset, M.: Hydrophobic Cluster Analysis of the Primary Sequences of alpha-Amylases , Intl J Biol Micromol 11, 217, 1989
• Elodi, P., Mora, S., and Krysteva, M.: Investigation of the Active Center of Porcine-Pancreatic Amylase , Eur J Biochem 24, 577, 1972
• Elser, R.: Comparison of Two Commercially Available Amylase Kits: Amylotube and Amylochrome , Clin Chem 21, 1854, 1975
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• Fridhandler, L., Berk, J., and Take, S.: Applicability of a New Synthetic Dye-Labeled Substrate for Amylase Assay , Proc Soc Exp Biol Med 133, 1212, 1970
• Fridhandler, L., Berk, J., and Ueda, M.: Isolation and Measurement of Pancreatic Amylase in Human Serum and Urine , Clin Chem 18, 1493, 1972
• Fujimori, H., Ohnishi, M., and Hiromi, K.: The Effects of Chemical Modification of N-Bromosuccinimide of Saccharifying alpha-Amylase from Bacillus subtilis on Various Substrates , J. Biochem. 75, 767, 1974
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• Garrett, C., Wilkinson, D., and Pitot, H.: Preparation of Ribonuclease-Free DNase I and alpha-Amylase , Anal Biochem 52, 342, 1973
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• Greenwood, C., MacGregor, A., and Milne, E.: The alpha-Amylase from Broad Beans. Purification and Properties , Arch Biochem Biophys 112, 459, 1965
• Groom, C., Daugulis, A., and White, B.: Continuous Alpha-Amylase Production Using Bacillus amyloliquefaciens Adsorbed on an Ion Exchange Resin, Appl Microbiol Biotechnol 28, 8, 1988
• Hafkenscheid, J., and Hessels, M.: Some Thermodynamic Parameters and Temperature-conversion Factors for Determining alpha-Amylase Concentration in Serum , Clin Chem 34, 2016, 1988
• Hafkenscheid, J., Hessels, M., and Wetzels, J.: Comparison of Two Methods for the Determination of the Isoenzymes of alpha-Amylase in Serum and Urine , Scand J Clin Lab Invest 49, 441, 1989
• Hamlin, C., and Schewede, K.: Standardization of an alpha-Amylase Kit Procedure , Clin Chem 20, 96, 1974
• Hao, J., Pazlarova, J., Strnadova, M., and Chaloupka, J.: Regulation of Extracellular Proteins and Alpha-Amylase Secretion by Temperature in Bacillus subtilis , Folia Microbiol (Praha) 34, 179, 1989
• Heller, J., and Schramm, M.: alpha-Amylase Limit Dextrins of High Molecular Weight Obtained from Glycogen, Biochim Biophys Acta 81, 96, 1964
• Hiatt, N.: Blood Glucose and Liver Glycogen C Following Intravenous Injection of Amylase , Proc Soc Exp Biol Med 119, 667, 1965
• Hiromi, K., Ohnishi, M., Kanaya, K., and Matsumoto, T.: The pH Jump Study of Enzyme Proteins. I. Liquefying alpha-Amylase from Bacillus subtilis , J. Biochem. 77, 957, 1975
• Holtzer, R., Van Lancker, J., and Swift, H.: Release of Amylase from Zymogen Granules and Microsomes , Arch Biochem Biophys 101, 439, 1963
• Hora, J.: Stabilization of Bacillus subtilis alpha-Amylase by Amino Group Acylation , Biochim Biophys Acta 310, 264, 1973
• Horigome, T., Kasai, H., and Okuyama, T.: The Stability of Taka-Amylase A Immobilized on Various Sizes of Matrix , J. Biochem. 75, 299, 1974
• Irie, A., Hunaki, M., Bando, K., and Kawai, K.: Activation of alpha-Amylase in Urine , Clin Chim Acta 51, 241, 1974
• Ishikawa, K., and Hirata, H.: New Substrate Specificity of Modified Porcine Pancreatic alpha-Amylase , Arch Biochem Biophys 272, 356, 1989
• Ishikawa, K., Matsui, I., and Honda, K.: Optimum pH Control Mechanism for Porcine Pancreatic a-Amylase , Biosci Biotechnol Biochem 59, 1175, 1995
• Ishikawa, K., Matsui, I., Honda, K., and Nakatani, H.: Substrate-Dependent Shift of Optimum pH in Porcine Pancreatic alpha-Amylase Catalyzed Reactions , Biochemistry 29, 7119, 1990
• Iwasa, S., Aoshima, H., Hiromi, K., and Hatano, H.: Subsite Affinities of Bacterial Liquefying alpha-Amylase Evaluated from the Rate Parameters of Linear Substrates , J. Biochem. 75, 969, 1974
• Janecek, S., and Balaz, S.: alpha-Amylases and Approaches Leading to Their Enhanced Stability , F.E.B.S. Lett. 304, 1, 1992
• Joseph, R., Oliver, E., and Ressler, N.: Electrophoretic Study of Human Isoamylases: A New Saccharogenic Staining Method and Preliminary Results , Gastroenterology 51, 377, 1966
• Kainuma, K., Kobayashi, S., Ito, T., and Suzuki, S.: Isolation and Action Pattern of Maltohexaose Producing Amylase from Aerobacter aerogenes , F.E.B.S. Lett. 26, 281, 1972
• Katoh, S., Terashima, M., and Miyaoku, K.: Purification of a-Amylase by Specific Elution From Anti-peptide Antibodies , Appl Microbiol Biotechnol 47, 521, 1997
• Khovrychev, M., Lirova, S., and Rabotnova, I.: Biosynthesis of Thermostable alpha-Amylase Under Continuous Cultivation, Microbiologia 56, 341, 1987
• Kobayashi, M., Takagi, S., Matsuda, K., and Ichishima, E.: Inhibition of alpha-Amylase and Phosphorylases by Cyclodextrin-Dialdehyde, Agric Biol Chem 52, 2703, 1988
• Kondo, H., Shiraishi, T., Nagata, K., and Tomita, K.: An Enzymatic Method for the alpha-Amylase Assay Which Comprises a New Procedure for Eliminating Glucose and Maltose in Biological Fluids , Clin Chim Acta 172, 131, 1988
• Kranz, D., Mutzbauer, H., and Schulz, G.: Determination of Sedimentation Coefficient, Diffusion Coefficient and Molecular Weight of alpha-Amylase According to the Activity Transport Method , Biochim Biophys Acta 102, 514, 1965
• Kruse-Jarres, J., Kaiser, C., Hafkenscheid, J., Hohenwallner, W., Stein, W., Bohner, J., Klein, G., Poppe, W., and Rauscher, E.: Evaluation of a New Alpha-Amylase Assay Using 4,6-Ethylidene-(G7)-1-4-Nitrophenyl-(G1)-Alpha-D-Maltoheptoside As Substrate , J Clin Chem Clin Biochem 2, 103, 1989
• Larson, S., Greenwood, A., Cascio, D., Day, J., and McPherson, A.: Refined Molecular Structure of Pig Pancreatic alpha-Amylase at 2-1 A Resolution , J Mol Biol 235, 1560, 1994
• Leloup, V., Colonna, P., and Marchismouren, G.: Mechanism of the Adsorption of Pancreatic Alpha-Amylase Onto Starch Crystallites , Carbohydr Res 232, 367, 1992
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• Levitzki, A., and Reuben, J.: Abortive Complexes of alpha-Amylases with Lanthanides , Biochemistry 12, 41, 1973
• Levitzki, A., and Steer, M.: The Allosteric Activation of Mammalian alpha-Amylase by Chloride , Eur J Biochem 41, 171, 1974
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• Longpre, J., and Hamel, M.: Evaluation of Chromogenic Substrate of Determining Amylase Activity in Serum , Circulation 6, 71, 1973
• Madi, E., and Antranikian, G.: Identification of a Starch Degrading Anaerobic Thermophile Producing Thermostable Alpha-Amylase and Pullulanase (Short Contribution), Appl Microbiol Biotechnol 30, 422, 1989
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• Moranelli, F., Yaguchi, M., Calleja, B. and Nasim, A.: Purification and Characterization of the Extracellular alpha-amylase Activity of the Yeast Schwanniomyces alluvius , Biochem Cell Biol 65, 899, 1987
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• Nitta, Y., Hiromi, K., and Ono, S.: Influence of Molecular Structures of Substrates and Analogues on Taka-Amylase A Catalyzed Hydrolyses. IIII. Inhibition by 2-Deoxy-D-Glucose and Methyl alpha-D-Glucoside: Change in Inhibition Type with Substrate Chain Length , J. Biochem. 70, 973, 1972
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• Ogden, J., O'Keefe, S., Ehlers, M., Kirsch, R., and Marks, I.: Single Step Affinity Chromatographic Purification of Human alpha-Amylase from Aspirated Duodenal Juice and Its Application in the Measurement of Pancreatic alpha-Amylase Synthesis Rates in Man , Clin Chim Acta 180, 129, 1989
• Ohnishi, M., Kegai, H., and Hiromi, K.: Studies on the Subsite Structure of Amylases. I. Interaction of Glucoamylase with Substrate and Analogues Studied by Difference-Spectrophotometry , J. Biochem. 77, 695, 1975
• Ohnishi, M., Kegai, H., and Hiromi, K.: Studies on the Subsite Structure of Amylases. II. Difference-Spectrophotometry Studies on the Interaction of Maltotriose with Liquefying alpha-Amylase from Bacillus subtilis , J. Biochem. 78, 2247, 1975
• Ohnishi, M., Suganuma, T., and Hiromi, K.: The Role of a Tyrosine Residue of Bacterial Liquefying alpha-Amylase in the Enzymatic Hydrolysis of Linear Substrates as Studied by Chemical Modification with Acetic Anhydride , J. Biochem. 76, 7, 1974
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• Omichi, K., Ikenaka, T., and Matsushima, Y.: Studies on the Substrate Specificity of Taka-Amylase A. XI. Effect of Release of p-Phenylazobenzoyl Residue from p-Phenylazobenzoyl Taka-Amylase A on the Enzymatic Action , J. Biochem. 73, 491, 1973
• Omichi, K., Kasai, and Matsushima, Y.: Studies on the Substrate Specificity of Taka-Amylase A. XII. Investigation of the Active Site of Taka-Amylase A by Examining the Properties of p-Phenylazobenzoyl Taka-Amylase A , J. Biochem. 78, 493, 1975
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• Ono, S., Hiromi, K., and Zinbo, M.: Kinetic Studies of Gluc-Amylase. I. The Influence of Chain Length of Linear Substrates on the Rate Parameters , J. Biochem. 55, 315, 1964
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• Pomeranz, Y.: Inactivation of alpha-Amylases by Synthetic Detergents , Biochim Biophys Acta 73, 105, 1963
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• Robyt, J., and French, D.: Multiple Attack Hypothesis of alpha-Amylase Action: Action of Porcine Pancreatic, Human Salivary, and Aspergillus oryzae alpha-Amylases , Arch Biochem Biophys 122, 8, 1967
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• Schumer, W.: Double Blind Study on the Use of Alpha-Amylase as an Antiinflammatory Agent , JAMA 181, 783, 1962
• Seigner, C., Prodanov, E., and Marchis-Mouren, G.: On Porcine Pancreatic alpha-Amylase Action: Kinetic Evidence for the Binding of Two Maltooligosaccharide Molecules (Maltose, Maltotriose, and O-Nitrophenylmaltoside) by Inhibition Studies - Correlation with the Five-Subsite Energy Profile , Eur J Biochem 148, 161, 1985
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