Linked Life Data

114282

Source:http://linkedlifedata.com/resource/pubmed/id/114282

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1979-12-18
pubmed:abstractText
Acid phosphatase activity in homogenized tibiae and femora of suckling rats was extracted with 0.3M KCl and 0.1% Triton X-100. A high-speed supernatant was treated with protamine sulfate, dialyzed, and chromatographed on CM-52 cellulose. All of the acid phosphatase activity was eluted with a sodium acetate buffer and combined ionic strength-pH gradient into two peaks (E1 and E2). Both enzyme peaks were further purified with Sephadex G-200, which resulted in 700- and 1000-fold purification for E2 and E1, respectively. A total of 220 units (mumoles substrate/min) of E2 with a specific activity of 160 units/mg protein has been obtained in one run by this procedure. E1 has a high molecular weight (greater than 100,000) and shows preference for monophosphate ester substrates, is markedly inhibited by tartrate, and has a pH optimum near 5. E2 has a lower molecular weight (greater than 40,000) and shows negligible activity with monophosphate esters [except with p-nitrophenyl phosphate (p-NPP)], but high activity with ADP and ATP. E2 is unaffected by tartrate and shows a pH optimum near 6. Both enzymes are competitively inhibited by inorganic phosphate, and E2, but not E1, is markedly inhibited by p-chloromercuribenzoate. With p-NPP as substrate, E1 and E2 have distinctly different values for Km. E1 appears similar to the high molecular weight acid phosphatases of soft tissues. However, E2 appears to differ from the low molecular weight phosphatases in soft tissues with regard to substrate specificity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0171-967X
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
219-26
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Purification and partial characterization of two acid phosphatases from rat bone.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.