Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A two-chain polypeptide, which corresponds to amino acid residues 115-143 and 144-184(185) of bovine serum albumin, connected to each other by a disulfide bridge, potentiated the effects of insulin on glucose transport and glucose metabolism in isolated rat adipocytes. Although the peptide alone had little activity, it shifted the concentration-response curves of insulin-stimulated D-[1-14C]glucose oxidation, 2-deoxyglucose transport, and lipid synthesis from D-[U-14C]glucose to lower insulin concentrations. It also increased the maximal responses of these parameters to insulin. However, it did not affect insulin binding to adipocytes. The peptide protected insulin considerably from degradation, but this effect alone cannot account for its effect in increasing the maximal responses to the hormone, and even when degradation of a submaximal concentration of insulin was suppressed by bacitracin, the peptide still had an enhancing effect. These results suggest not only that the peptide influences a step distal to receptor-mediated insulin binding but also that inhibition of insulin degradation alone cannot explain its total effect. The peptide lost its insulin-stimulating activity completely when it was further digested with V8 or lysine-specific endopeptidase, or when it was reduced and then carboxamidomethylated or oxidized with performic acid. Similar active tryptic fragments were obtained from human and rat albumins. Insulin-stimulating peptides should be useful in studies on the mechanisms of insulin action including both the sensitivities and responsiveness of target cells to the hormone.
Mol Cell Biochem 1986 May
PMID:Studies on the biological activity of an insulin-stimulating peptide from a tryptic digest of bovine serum albumin. 352 9

A specific antibody subpopulation(s) in antihorse cytochrome c serum was detected for peptide fragment 81-104 of cyanogen bromide (CNBr) cleaved horse cytochrome c (HCytc). This antiserum was made in the rabbit against polymeric horse cytochrome c. The presence of the peptide-specific antibody subpopulation(s) was demonstrated utilizing HCytc, CNBr-peptide 81-104 and isolated chymotrypsin-digested HCytc fragments 60-67, 83-97 and 98-104 to compete with radio-labeled peptide 81-104 and antiHCytc serum in a competitive radioimmunoassay (RIA). This antibody subpopulation(s) in antiHCytc serum was demonstrated to be specific for peptide 81-104. At the 50% inhibition level in competitive RIA, 100- and 1000-fold molar excesses of HCytc and its peptide 1-65, respectively, were required to affect an equivalent binding to that of the HCytc peptide 81-104. Competitive RIAs have been performed utilizing three different kinds of antigen to compete with HCytc peptide 81-104 and antihorse cytochrome c sera. These three kinds of antigens are: endopeptidase digests of HCytc, cytochrome c peptides 81-104 of several species and several isolated chymotryptic peptide fragments of HCytc. The results have indicated that this peptide-specific antibody subpopulations(s) in antiHCytc serum is similar to antibodies made against peptide 81-104-BSA. Regions of antigenicity have been identified at positions 92, 100, 103 and 104 with both antisera.
Mol Immunol 1984 Oct
PMID:Antibody subpopulation in antihorse cytochrome c serum. 620 69

Two mutants of Escherichia coli that are deficient in the penicillin-insensitive DD-endopeptidase have been isolated. The strain JE10874 (mepA) has about 10%-20% of the residual activity and another strain, JE10368 (mepB) has 40%-50% of the activity found in the wild-type, parental strain, PA3092. The penicillin-insensitive endopeptidase is a periplasmic enzyme. Genetic mapping studies show that the mutation mepA is located close to aroC (50 min) and the other mutation, mepB, is very close to malE (91 min) on the chromosome. These mutants grow normally under a wide range of growth conditions; other phenotypic properties of the mutants are very similar to those of the parent strain. A double mutant (mepA mepB), and a triple mutant (mepA mepB dacB), deficient in both penicillin-insensitive and penicillin-sensitive endopeptidases, were constructed. Again, these mutants grew normally. We conclude that either the very low level of residual enzyme activity in the mutants is enough for their survival or that the penicillin-insensitive endopeptidase is not essential for survival under laboratory conditions.
Mol Gen Genet 1983
PMID:Mutants of Escherichia coli defective in penicillin-insensitive murein DD-endopeptidase. 634 88

Monoclonal antibodies generated against normal and leukemic human leukocytes were tested for their differential reactivity with leukemia and lymphoma cell lines as well as with circulating lymphoid and myeloid leukemic cells by means of immuno-scanning electron microscopy (immuno-SEM). Anti-T (OKT3), anti-mu-chain, anti-CALLA (J5), anti-BA-1, anti-BA-2, and anti-nonlymphoid (Mol) monoclonal antibodies were covalently conjugated to polystyrene latex microspheres (immunolatex), using a two-step glutaraldehyde reaction, and subsequently incubated with the various cell types. Cultured B-type Burkitt lymphoma cells (Daudi) and chronic lymphocytic leukemia (CLL) cells displayed extensive labeling with monoclonal anti-mu, anti-B1, and anti-BA-1 immunolatex conjugates, while cultured malignant T cells (HD-Mar) showed positive labeling with OKT3 immunolatex alone. Cultured myelomonocytic cells (GDM-1) and cells obtained from patients with acute myeloblastic (AML) and monoblastic leukemia (AMoL) labeled only with anti-Mol immunolatex, while cultured promyelocytic cells (HL-60) displayed far less labeling with this conjugate. Common-type acute lymphoblastic leukemia (C/ALL) cells were labeled predominantly with the J5 (anti-CALLA) and anti-BA-2 immunolatex conjugates. Evidence is presented indicating that immuno-SEM employing monoclonal antibodies is a reproducible technique which may be used in the study of leukocyte maturation and may provide additional information in the classification of poorly differentiated leukemias.
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PMID:Utilization of monoclonal antibodies and immuno-scanning electron microscopy for the positive identification of human leukemic cells. 658 Nov 72

Peptidases which are specific for proline residues have been described and include endopeptidases (post-proline cleaving enzyme and proline specific endopeptidase), N-terminal exopeptidases (post-proline dipeptidyl aminopeptidase, proline iminopeptidase, aminopeptidase P), C-terminal exopeptidases (prolylcarboxypeptidase, and carboxypeptidase P) and dipeptidases (prolyl dipeptidase and proline dipeptidase). The properties, distinguishing charcteristics, and possible significance of these proline specific endo- and exopeptidases are discussed. In addition, reference is made to a series of enzymes which can hydrolyze proline containing peptide bonds, but which are not specific for proline.
Mol Cell Biochem 1980 Apr 18
PMID:Proline specific endo- and exopeptidases. 699 12

An acid peptidase that degrades hemoglobin optimally at pH 3.5, a neutral aminopeptidase and an alkaline endopeptidase that acts on an alpha-N-blocked synthetic substrate have been demonstrated in Plasmodium falciparum in culture. The enzymes were shown to be distinct by anion exchange chromatography, gel filtration on Sephadex G-200 and isoelectric focusing. The activities of the acid peptidase and the aminopeptidase were inhibited by antimalarial compounds.
Mol Biochem Parasitol 1982 Apr
PMID:Peptidases from Plasmodium falciparum cultured in vitro. 704 89

This computational study is a summary of how cloned beta-glucosidase subfamilies are organized. Computations were carried out using General Computer Group, Inc. (GCG) package programs. Twenty-two beta-glucosidases belonging to either cellulolytic or non-cellulolytic organisms were identified. The multialignment of a whole beta-glucosidase family is shown. Two sub-families, A and B, were clearly seen to exist. Sub-family A is further subdivided into sub-families A1 and A2. A1 includes vegetal beta-glucosidases and A2 includes prokaryotic enzymes. Sub-family B has three new sub-families, B1, B2, and B3. The enzymes in B2 are of yeast and/or fungi. Aspartic (D), glutamic (E) and histidine (H) residues, which are thought to be a part of the mechanism of the enzymatic hydrolysis are conserved. The well conserved amino acid sequences of the sub-family A are ITENGA; QUIEGA; HVD; and NEP. The well conserved amino acid sequences of the sub-family B are: SDW; and YN(R,K)(V,L)N.
Biochem Mol Biol Int 1995 May
PMID:beta-Glucosidase families revealed by computer analysis of protein sequences. 749 60

Respiratory epithelial cell surface neutral endopeptidase 24.11 (NEP-24.11) degrades proinflammatory peptides, and it has been suggested that glucocorticoids may reduce airway inflammation, in part, by upregulation of NEP-24.11. Despite the potential importance of the epithelium as a metabolic barrier, little is known regarding what other peptidases may be present on the epithelial cell surface. Using an immortalized bronchial epithelial cell line (BEAS-2B), we have shown that human epithelial cells express no detectable angiotensin-converting enzyme, carboxypeptidase N, or dipeptidyl(amino)peptidase IV, but express significant levels of aminopeptidase M (AmM), as well as NEP-24.11. The presence of these enzymes was demonstrated via their degradation of biologically active peptides and by flow cytometry. Exposure of cells to the glucocorticoid budesonide (10(-7) M) for up to 5 days did not markedly alter the expression of NEP-24.11 or AmM, as assessed by flow cytometry, nor did glucocorticoid treatment modify rates of peptide hydrolysis by NEP-24.11 or AmM. Thus, BEAS-2B cells have both AmM and NEP-24.11 on their surface, and expression of these enzymes is not altered by glucocorticoids.
Am J Respir Cell Mol Biol 1994 Jul
PMID:Glucocorticoids do not alter peptidase expression on a human bronchial epithelial cell line. 751 43

Botulinum neurotoxin C1 inhibited Ca(2+)-evoked norepinephrine secretion from digitonin-permeabilized PC12 cells. The inhibition by the neurotoxin was dependent on the presence of Zn2+ added exogenously. This zinc-dependent inhibition was neutralized by monoclonal antibodies that recognize the sites close to the putative zinc-binding motif in the light chain. The neurotoxin was found to have an endopeptidase activity toward small peptide, substance P. The presence of exogenous Zn2+ was also indispensable to the full expression of this endopeptidase activity. Thus both the inhibition of neurotransmitter release by the C1 neurotoxin and its endopeptidase activity are dependent on exogenous Zn2+, which suggests a strong link between the two activities.
Biochem Mol Biol Int 1994 Mar
PMID:Exogenous zinc ion is required for inhibitory activity of botulinum neurotoxin C1 against norepinephrine release and its endopeptidase activity toward substance P. 751 76

Plasma very-low density lipoprotein (VLDL) and vitellogenin (VTG) from mature female Japanese quail (Coturnix coturnix japonica) and chickens (Gallus domesticus) were isolated and digested in vitro with cathepsin D (EC3.4.23.5). The incubation mixtures were then reduced and subjected to gradient (4.5-18%) SDS-polyacrylamide gel electrophoresis. Protein fragments were stained with either Coomassie Brilliant Blue R-250 (VLDL digests) or Coomassie Brilliant Blue R-250 containing 20 mM AlCl3 (VTG digests). Fragments resulting from the in vitro enzymatic digestion of quail and chicken plasma VLDL-apolipoprotein B (apo B) and VTG closely resembled those produced in vivo and isolated from egg yolks of each respective species. Phosvitin, a proteolytically derived fragment of VTG, primarily existed as a single band (M(r) approximately 42 kDa) in Japanese quail yolk granules. In contrast, chicken phosvitin mainly consisted of a cluster of phosphoproteins ranging in size from approximately 37 to 45 kDa. In addition to reporting a novel species difference in phosvitin moieties, the present study is the first to examine the role of cathepsin D in the generation of egg yolk proteins from plasma precursors in Japanese quail. Confirmatory evidence also was provided concerning the important role of this aspartic endopeptidase in the proteolytic cleavage of plasma VLDL-apo B and VTG in the chicken.
Comp Biochem Physiol B Biochem Mol Biol 1995 Oct
PMID:Proteolysis of Japanese quail and chicken plasma apolipoprotein B and vitellogenin by cathepsin D: similarity of the resulting protein fragments with egg yolk polypeptides. 758 50


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