Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1976-7-6
pubmed:abstractText
The unicellular alga Chlamydomonas reinhardi produces two constitutive acid phosphatases and three depressible phosphatases (a neutral and two alkaline ones) that can utilize napthyl phosphate as a substrate. Specific mutants depressible phosphatase were used to investigate biochemical properties and the cytochemical localization of these enzymes. The two constitutive phosphatases show similar pH optima (about 5.0) and Km values (2 x 10(-3) to 3.3 x 10(-3) M) but differ in their heat sensitivity and affinity for glycerophosphate.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-14326109, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-167670, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-236977, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-4291397, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-4357315, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-4426925, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-4559833, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-4565542, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-4778787, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-4811547, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-5055814, http://linkedlifedata.com/resource/pubmed/commentcorrection/4437-5582063
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
937-50
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Phosphatase of Chlamydomonas reinhardi: biochemical and cytochemical approach with specific mutants.
pubmed:publicationType
Journal Article