Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1975-5-21
pubmed:abstractText
Two molecular forms of carbonic anhydrase were identified in the rat anterior pituitary gland. Electrophoretic and immunological studies disclosed that the low activity carbonic anhydrase (type B) was associated with the particulate fraction of the pituitary gland and the high activity carbonic anhydrase (type C) was localized in the soluble fraction. The 800 times g pellet contained 50% of the total activity of a pituitary homogenate prepared in 0.25 M sucrose, while the 105,000 times g supernatant accounted for an additional 30% of the total. The particulate enzyme was rendered soluble by treatment with Trition X-100. The activity of pituitary gland carbonic anhydrase was about 6 times greater in preparations from female rats as compared with males. The activity of carbonic anhydrase in the particulate fraction decreased, and the activity in the soluble fraction increased without a change in total activity following incubation in vitro of pituitary glands. The intracellular adjustment in enzyme activity was accompanied by the secretion of prolactin into the incubation medium by the pituitary gland. The secretion of prolactin and the solubilization of the particulate carbonic anhydrase was inhibited when the pituitary gland was incubated in the presence of 10-5 M dopamine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
250
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1933-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Evidence of existence of two isozymes of carbonic anhydrase in the anterior pituitary gland of female rats.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.