Mosaic lectin and enzyme staining patterns in rat skeletal muscle.
J Histochem Cytochem
; 40(10): 1511-6, 1992 Oct.
Article
en En
| MEDLINE
| ID: mdl-1382089
ABSTRACT
We compared the localizations of lectin binding and activity for myosin ATPase and succinic dehydrogenase in sections of the gracilis, soleus, and masseter muscles from 10- and 60-day-old rats. In the 60-day-old rats, incubation of the muscle sections with the lectins ConA, GS-II, HPA, and jacalin gave rise to a mosaic staining pattern, especially in the gracilis muscle, in which the same fibers were strongly stained for ConA, GS-II, and HPA, whereas the staining with jacalin in these fibers was weak, and vice versa. There was no correspondence in the staining patterns for the enzymes and the lectins. In the masseter muscle only GS-II gave rise to distinct differences in the staining intensity between muscle fibers. In 10-day-old rats all fibers in the muscles were moderately stained with ConA, HPA, and jacalin, whereas a chessboard staining pattern could be observed after incubation with GS-II. In an extract of hindleg muscle from 60-day-old rats there was strong affinity for ConA and HPA and weak affinity for GS-II and jacalin, as shown by dot-blotting. After electrophoresis and blotting to nitrocellulose membranes, three muscle protein bands with apparent molecular weights of 100,000, 90,000, and 43,000 showed affinity for ConA, HPA, and GS-II, whereas no bands were jacalin positive. The complex lectin staining pattern in skeletal muscle might be related to development, specialization, and function of the muscles.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Succinato Deshidrogenasa
/
Miosinas
/
Lectinas
/
Músculos
Límite:
Animals
Idioma:
En
Revista:
J Histochem Cytochem
Asunto de la revista:
HISTOCITOQUIMICA
Año:
1992
Tipo del documento:
Article
País de afiliación:
Dinamarca