J. Berzelius (Ms. Esslinger, trans.), Traité de Chimie (París, Francia: Firmin Didot Frerès, 1833), vol. 7, page 156.
doi.org
dx.doi.org
Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ (maio de 1996). "Structure of human salivary α-amylase at 1.6 Å resolution: implications for its role in the oral cavity". Acta Crystallographica D52 (Pt 3): 435–46. PMID15299664. doi:10.1107/S0907444995014119.
Fried M, Abramson S, Meyer JH (outubro de 1987). "Passage of salivary amylase through the stomach in humans". Digestive Diseases and Sciences32 (10): 1097–103. PMID3652896. doi:10.1007/bf01300195.
Rosenblum JL, Irwin CL, Alpers DH (maio de 1988). "Starch and glucose oligosaccharides protect salivary-type amylase activity at acid pH". The American Journal of Physiology254 (5 Pt 1): G775–80. PMID2452576. doi:10.1152/ajpgi.1988.254.5.G775.
Granger DA, Kivlighan KT, el-Sheikh M, Gordis EB, Stroud LR (marzo de 2007). "Salivary α-amylase in biobehavioral research: recent developments and applications". Annals of the New York Academy of Sciences1098 (1): 122–44. Bibcode:2007NYASA1098..122G. PMID17332070. doi:10.1196/annals.1384.008.
Nater UM, Rohleder N (maio de 2009). "Salivary α-amylase as a non-invasive biomarker for the sympathetic nervous system: current state of research". Psychoneuroendocrinology34 (4): 486–96. PMID19249160. doi:10.1016/j.psyneuen.2009.01.014.
Ghalanbor Z, Ghaemi N, Marashi SA, Amanlou M, Habibi-Rezaei M, Khajeh K, Ranjbar B (2008). "Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity". Protein and Peptide Letters15 (2): 212–4. PMID18289113. doi:10.2174/092986608783489616.
Abe A, Yoshida H, Tonozuka T, Sakano Y, Kamitori S (decembro de 2005). "Complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages". The FEBS Journal272 (23): 6145–53. PMID16302977. doi:10.1111/j.1742-4658.2005.05013.x.
Kadziola A, Søgaard M, Svensson B, Haser R (abril de 1998). "Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis". Journal of Molecular Biology278 (1): 205–17. PMID9571044. doi:10.1006/jmbi.1998.1683.
Kadziola A, Abe J, Svensson B, Haser R (maio de 1994). "Crystal and molecular structure of barley α-amylase". Journal of Molecular Biology239 (1): 104–21. PMID8196040. doi:10.1006/jmbi.1994.1354.
Machius M, Wiegand G, Huber R (marzo de 1995). "Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution". Journal of Molecular Biology246 (4): 545–59. PMID7877175. doi:10.1006/jmbi.1994.0106.
harvard.edu
adsabs.harvard.edu
Granger DA, Kivlighan KT, el-Sheikh M, Gordis EB, Stroud LR (marzo de 2007). "Salivary α-amylase in biobehavioral research: recent developments and applications". Annals of the New York Academy of Sciences1098 (1): 122–44. Bibcode:2007NYASA1098..122G. PMID17332070. doi:10.1196/annals.1384.008.
lsbu.ac.uk
www1.lsbu.ac.uk
"The use of enzymes in detergents". Faculty of Engineering, Science and the Built Environment, London South Bank University. 20 de decembro de 2004. Arquivado dende o orixinal o 20 de outubro de 2009. Consultado o 21 de novembro de 2009.
nih.gov
ncbi.nlm.nih.gov
Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ (maio de 1996). "Structure of human salivary α-amylase at 1.6 Å resolution: implications for its role in the oral cavity". Acta Crystallographica D52 (Pt 3): 435–46. PMID15299664. doi:10.1107/S0907444995014119.
Fried M, Abramson S, Meyer JH (outubro de 1987). "Passage of salivary amylase through the stomach in humans". Digestive Diseases and Sciences32 (10): 1097–103. PMID3652896. doi:10.1007/bf01300195.
Rosenblum JL, Irwin CL, Alpers DH (maio de 1988). "Starch and glucose oligosaccharides protect salivary-type amylase activity at acid pH". The American Journal of Physiology254 (5 Pt 1): G775–80. PMID2452576. doi:10.1152/ajpgi.1988.254.5.G775.
Granger DA, Kivlighan KT, el-Sheikh M, Gordis EB, Stroud LR (marzo de 2007). "Salivary α-amylase in biobehavioral research: recent developments and applications". Annals of the New York Academy of Sciences1098 (1): 122–44. Bibcode:2007NYASA1098..122G. PMID17332070. doi:10.1196/annals.1384.008.
Nater UM, Rohleder N (maio de 2009). "Salivary α-amylase as a non-invasive biomarker for the sympathetic nervous system: current state of research". Psychoneuroendocrinology34 (4): 486–96. PMID19249160. doi:10.1016/j.psyneuen.2009.01.014.
Ghalanbor Z, Ghaemi N, Marashi SA, Amanlou M, Habibi-Rezaei M, Khajeh K, Ranjbar B (2008). "Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity". Protein and Peptide Letters15 (2): 212–4. PMID18289113. doi:10.2174/092986608783489616.
Abe A, Yoshida H, Tonozuka T, Sakano Y, Kamitori S (decembro de 2005). "Complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages". The FEBS Journal272 (23): 6145–53. PMID16302977. doi:10.1111/j.1742-4658.2005.05013.x.
Kadziola A, Søgaard M, Svensson B, Haser R (abril de 1998). "Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis". Journal of Molecular Biology278 (1): 205–17. PMID9571044. doi:10.1006/jmbi.1998.1683.
Kadziola A, Abe J, Svensson B, Haser R (maio de 1994). "Crystal and molecular structure of barley α-amylase". Journal of Molecular Biology239 (1): 104–21. PMID8196040. doi:10.1006/jmbi.1994.1354.
Machius M, Wiegand G, Huber R (marzo de 1995). "Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution". Journal of Molecular Biology246 (4): 545–59. PMID7877175. doi:10.1006/jmbi.1994.0106.
"The use of enzymes in detergents". Faculty of Engineering, Science and the Built Environment, London South Bank University. 20 de decembro de 2004. Arquivado dende o orixinal o 20 de outubro de 2009. Consultado o 21 de novembro de 2009.