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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1993-5-21
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pubmed:abstractText |
Human pancreatic alpha-amylase has been isolated using a glycogen affinity precipitation procedure and crystallized in a form suitable for high resolution three-dimensional X-ray crystallographic analyses. Crystals are of the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 53.04 A, b = 74.80 A and c = 137.34 A, and contain only one protein molecule per asymmetric unit. Diffraction data have been collected and found to extend to 1.6 A resolution. These studies form the basis for elucidating the full atomic structure of human pancreatic alpha-amylase and thereby providing insight into the catalytic mechanism of this enzyme.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0022-2836
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
5
|
pubmed:volume |
230
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1084-5
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading | |
pubmed:year |
1993
|
pubmed:articleTitle |
Isolation, crystallization and preliminary diffraction analyses of human pancreatic alpha-amylase.
|
pubmed:affiliation |
Department of Biochemistry, University of British Columbia, Vancouver, Canada.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|