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Results for “Peptide Mapping”

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At least 505 records · Page 28Linked to original sources
PubMed1983

Phosphorylation site specificities of glycogen synthase kinases: determination by peptide mapping using high-performance liquid chromatography.

A method is described which separates the various phosphorylation sites in glycogen synthase based on reverse phase high-performance liquid chromatography (HPLC) of tryptic 32P-peptides. Using this method we studied the phosphorylation site specificities of the kinases which act on glycogen synthase. The cAMP-dependent protein kinase phosphorylated sites 1a, 1b, and 2, whereas casein kinase II phosphorylated only site 5. Two calcium, calmodulin-dependent kinases, phosphorylase kinase and liver calmodulin-dependent synthase kinase, both phosphorylated site 2, and the latter enzyme also phosphorylated site 1b. A cAMP-independent kinase (kinase 4) purified from liver also specifically phosphorylated site 2. Synthase kinase 3 catalyzed the phosphorylation of only site 3. This HPLC method was also used to establish that all of these sites were subject to phosphorylation in vivo.

Animals↗
PubMed1983

Classification of tropomyosin components into an alpha-like or a beta-like family by partial peptide mapping.

Tropomyosins can be classified as belonging to an alpha-like or a beta-like family depending on the absence or presence, respectively in their protease-V8 digestion pattern of two peptides with an apparent molecular mass of 21 kDa. Chicken cardiac tropomyosin and the 43 kDa component from gizzard tropomyosin are accordingly classified as alpha-like tropomyosins, while the 33 kDa gizzard tropomyosin component is a beta-like tropomyosin. The 21 kDa peptides have an overall charge which is more positive than that of the intact tropomyosin or any other tropomyosin peptide and probably contain the -NH2 half of the molecule.

Animals↗
PubMed1996

Antibody against synthetic multiple antigen peptides (MAP) of JC virus capsid protein (VP1) without cross reaction to BK virus: a diagnostic tool for progressive multifocal leukoencephalopathy.

Antibody against JC virus (JCV) was raised in rabbits with the use of synthetic multiple antigen peptides. The peptide sequences were derived from three regions of JCV VP1 protein, which showed less similarity with BK virus (BKV) counterpart. The antibodies raised with these peptides were designated as JCAb1, 2 and 3. JCAb1 specifically reacted with JCV and not with BKV, while JCAb2 and 3 reacted both with JCV and BKV. All of these antibodies reacted with JCV antigen of formalin-fixed paraffin sections of progressive multifocal leukoencephalopathy (PML) brain tissue. As JCAb1 is JCV-specific and reacted with JCV in formalin-fixed paraffin sections, it will contribute not only to rapid and accurate immunohistochemical diagnoses of PML but also to clarification of the pathogenesis of JCV infection.

Amino Acid Sequence↗
PubMed1981

Bovine hypothalamic poly(A)-rich RNA-directed synthesis of a common precursor to the nonapeptide arginine vasopressin and neurophysin II. Immunological identification and tryptic peptide mapping.

The common precursor to arginine vasopressin (AVP) and neurophysin II (NpII) has been synthesized in a reticulocyte lysate system directed by bovine hypothalamic poly(A)-rich RNA. The precursor, identified with antibodies raised against neurophysin II and arginine vasopressin, has an apparent Mr of 21 000 (21 k). The specificity of the immune reaction has been shown by competition experiments using excess amounts of a variety of unlabeled peptides. With anti Np II, but not with anti AVP, a second neurophysin precursor with an apparent Mr of 18 000 (18 k) has been identified. Comparison of the tryptic maps obtained from the 21 k and 18 k precursors shows that both products give rise to the four [35S]cysteine-labeled neurophysin II-peptide fragments; however, only the 21 k yields an AVP-like tryptic peptide, identified with antibodies raised against AVP. The possible implications of the two precursors, one consisting of AVP and Np II, the other of Np II only, are discussed.

Animals↗