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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1988-6-9
|
| pubmed:abstractText |
We examined by means of the immunoblotting technique the transition of beta-actinin isoforms during the development of the chicken from 5 day embryo to adult. As an antigen, beta-actinin was prepared from adult chicken breast muscle (pectoralis major) and polyclonal antibody was obtained by injecting undenatured beta-actinin into a rabbit. Immunoblotting examination of breast muscle at several stages of development (except 5 day embryo, in which the whole body minus the head and limbs was examined) showed that the species of beta-actinin subunits change during development: 1) beta I is already present in 5 day embryo, whereas beta II appears only after 9 days. 2) In 5 day embryo, we found, instead of beta II, a new subunit (designated beta III) that cross-reacts with the antibody, has the apparent molecular weight of 30,000 daltons and has a slightly alkaline isoelectric point compared with beta I. The content of beta III gradually decreased and beta III completely disappeared a week after hatching. Such a type of transition of the isoforms in beta-actinin subunits is similar to that observed in other muscle proteins. The transition of beta-actinin isoforms may correlate to the organization of an I-Z-I brush, especially to the length determination of thin filaments, because the developmental stage at which beta III disappears coincides with that at which the length of thin filaments is strictly determined.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-924X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
103
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
72-5
|
| pubmed:dateRevised |
2007-12-19
|
| pubmed:meshHeading | |
| pubmed:year |
1988
|
| pubmed:articleTitle |
Transition of beta-actinin isoforms during development of chicken skeletal muscle.
|
| pubmed:affiliation |
Department of Physics, School of Science and Engineering, Waseda University, Tokyo.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|