Seed germination studies I. Purification and properties of an [alpha]-amylase from the cotyledons of germinating peas
dc.contributor.author | Swain, Richard R. | en_US |
dc.contributor.author | Dekker, Eugene E. | en_US |
dc.date.accessioned | 2006-04-17T16:15:31Z | |
dc.date.available | 2006-04-17T16:15:31Z | |
dc.date.issued | 1966-07-06 | en_US |
dc.identifier.citation | Swain, Richard R., Dekker, Eugene E. (1966/07/06)."Seed germination studies I. Purification and properties of an [alpha]-amylase from the cotyledons of germinating peas." Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation 122(1): 75-86. <http://hdl.handle.net/2027.42/33426> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GG-47T8XMM-8/2/24f409e8ee011aee892d5c7dfef895de | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/33426 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5968175&dopt=citation | en_US |
dc.description.abstract | A starch-hydrolyzing enzyme present in extracts of the cotyledons of germinating peas has been purified over 3400-fold. Several independent criteria show that this activity is due to an amylase of the [alpha]-type ([alpha]-1,4-glucan-4-glucanohydrolase, EC 3.2.1.1). The enzyme exhibits maximal activity in the pH range 5.3-5.9; the Michaelis constant (Km) and energy of activation (Ea) for the enzyme-catalyzed reaction are 2[middle dot]10-4 g soluble starch per ml and 7600 cal/mole, respectively. Calcium ions protect the amylase against heat inactivation, whereas incubation of the enzyme with 5[middle dot]10-4 M EDTA for 20 min at room temperature results in complete loss of activity. With amylose and amylopectin as substrates, this enzyme is similar in action pattern to other known plant [alpha]-amylases. | en_US |
dc.format.extent | 852467 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Seed germination studies I. Purification and properties of an [alpha]-amylase from the cotyledons of germinating peas | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich., U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich., U.S.A. | en_US |
dc.identifier.pmid | 5968175 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/33426/1/0000828.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0926-6593(66)90092-0 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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