Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Drug
Enzyme
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Query: EC:3.4.21.1 (
chymotrypsin
)
10,938
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
We examined the association of a 34-kD light chain component to the heavy chains of
MAP-1
using a monoclonal antibody that specifically binds the 34-kD component and labels neuronal microtubules in a specific and saturable manner. Immunoprecipitation of
MAP-1
heavy chains together with the 34-kD component by the antibody indicates that the 34-kD polypeptide forms a complex with
MAP-1
heavy chains. Both major isoforms of
MAP-1
heavy chains (MAP-1A and MAP-1B) were found in the immunoprecipitate. Digestion of
MAP-1
with
alpha-chymotrypsin
and analysis of the chymotryptic peptides reveals a 120-kD fragment of the
MAP-1
heavy chain that binds to microtubules and is precipitable with the 34-kD light chain antibody, suggesting that the 34-kD light chain also binds to this domain of the molecule. Since microtubules that contain the 120-kD fragment lack the long lateral projections characteristic of microtubules with intact
MAP-1
, the 34-kD light chains may be localized at or near the microtubule surface.
...
PMID:Identification of a 34-kD polypeptide as a light chain of microtubule-associated protein-1 (MAP-1) and its association with a MAP-1 peptide that binds to microtubules. 351 77
The major high molecular weight microtubule-associated polypeptides from hog brain (
MAP-1
and MAP-2) were compared by one- and two-dimensional peptide mapping under varied conditions and by immunological techniques. Partial digestion of
MAP-1
and MAP-2 with Staphylococcus aureus V8 protease and analysis in one dimension gave rise to very similar peptide maps independent of whether 125I-, 3H-, or 32P-labeled proteins were used. One-dimensional cleavage patterns of significant similarity were also obtained by partial digestion of
MAP-1
and MAP-2 using trypsin or
chymotrypsin
. Furthermore, a pronounced similarity, although clear nonidentity, of
MAP-1
and MAP-2 was also revealed after exhaustive digestion of 125I-labeled proteins with S. aureus V8 protease or trypsin followed by analysis of peptides in two dimensions. For immunological comparison, antisera were used that had been raised in rabbits using electrophoretically purified
MAP-1
and MAP-2 components as immunogens. As determined by immunoprecipitation, the antiserum raised to
MAP-1
was equally reactive with
MAP-1
and MAP-2 components, whereas the antiserum to MAP-2 reacted primarily with MAP-2. Indicating the presence of common as well as unique antigenic determinants on
MAP-1
and MAP-2, these results, therefore, were in agreement with the peptide mapping data. Implications of these results for biosynthetic mechanisms as well as differential distribution and functions of MAPs in cells are discussed.
...
PMID:Structural homology of microtubule-associated proteins 1 and 2 demonstrated by peptide mapping and immunoreactivity. 636 43
