Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1976-10-20
pubmed:abstractText
A hybrid enzyme (LI) of liver phosphorylase [EC 2.4.1.1.] (L) and phosphorylase I, which is mainly located in brain, was isolated and its enzymatic and immunological properties were examined. The following results were obtained: (1) AMP stimulated the b forms of the hybrid (LIb), I(Ib), and L(Lb); (2) in the presence of AMP, SO42- stimulated Lb more than LIb and inhibited Ib; (3) in the absence of AMP, SO42- stimulated all three isozymes in the order: Ibeta less than LI less than Lbeta; (4) on conversion to the a forms, the activities of L, LI, and I increased 35.5-fold, 3-fold, and 1.2-fold, respectively; (5) the relative inhibition potencies of anti-Lb antibody with LIa and LIb were 63% and 4%, respectively of that with La, and those of anti-Ib antibody with LIa and LIb were 42% and 88%, respectively of that with Ia. Since the ratios of the specific activities of purified La and Ia and of Lbeta and Ibeta are 70: 82 and 2 : 70, respectively (Schliselfeld, 1973), the present findings suggest a 1 : 1 association of I and L subunits in the hybrid molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1109-11
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Hybrid enzyme of liver phosphorylase and phosphorylase I.
pubmed:publicationType
Journal Article