Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1985-8-29
pubmed:abstractText
Constitutive acid phosphatase was purified from yeast cells grown in a medium supplied with 100 mM phosphate. Specific activity of the pure enzyme was 63.5 mumol/min X mg. The enzyme contains 42.5% of protein, 55% of mannose and 2.5% of N-acetylglucosamine. The carbohydrate chains are N-glycosidically linked to the protein. The pure enzyme shows non-linearity in the Lineweaver-Burk plot, thus indicating the presence of two enzyme forms with Km values of about 0.65 mM and 8.5 mM. The pH optimum of the enzyme is at pH 3.3. The enzyme is much more sensitive to heat denaturation than the repressible acid phosphatase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
567-75
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Purification, carbohydrate composition and kinetic properties of the constitutive yeast acid phosphatase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't