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)

Peptidases capable of releasing proline residues from polypeptides are present in the cytoplasmic fraction of rabbit polymorphonuclear granulocytes. This was shown with peptide substrates where proline is present either at the carboxy-terminal or within the polypeptide chain. Lysosomal and plasma membrane enzymes were inactive towards such polypeptides. The proline residue was hydrolyzed at either its amino end or its carboxy end. It is noteworthy that a Pro:Pro bond was cleaved both in the pentapeptide Thr-Lys-Pro-Arg and the dipeptide Pro:Pro.
Mol Cell Biochem 1976 Feb 16
PMID:Proline endopeptidase and exopeptidase activity in polymorphonuclear granulocytes. 0 27

Amylase from chicken pancreas was purified by an affinity method involving filtering a crude extract from pancreas through a Sepharose-wheat albumin column and eluting the retained enzyme with maltose. The purified amylase showed two active bands upon polyacrylamide electrophoresis in an alkaline buffer system and only one band in an acidic buffer system. The enzyme is a Ca2+-glycoprotein which behaves as a typical alpha-amylase. It consists of a single polypeptide chain with molecular weight 53,000 and contains 5.3 moles of reducing sugars per mole of protein. Optimal conditions of pH and temperature for the enzymic activity are 7.5 and 37 degrees C. The enzyme is irreversibly inactivated by removal of Ca2+ by exhaustive dialysis and is activated by the presence in the assay mixture of Cl-; other halides are less effective than Cl- in activating the enzyme.
Mol Cell Biochem 1977 Aug 19
PMID:Purification and properties of alpha-amylase from chicken (Gallus gallus L.) pancreas. 2 May 68

Alteration of the intermolecular interaction in aqueous solution of human serum albumin (SA) as a result of the increase of ionic strength and pH values brings about the slowing-down of the spin-echo decay curve for protein protons (several times at high SA concentrations). A specific effect of alkaline pH was observed, i.e. the slowing-down of quick component of the spin-echo decay curve. This result taken together with the data on complex spin-echo decay curve, correlation times of protons of different regions is SA and compared with SA isotope exchange data can be explained as a result of the polypeptide chain conformation mobility with frequencies more 10(4) c.p.s. This effect is observed in regions occupying about one half of the SA macromolecule volume.
Mol Biol (Mosk)
PMID:[NMR spin-echo study of behaviour dynamics of serum albumin macromolecules in aqueous solutions as a function of pH and ionic strength]. 3 29

lambda infected minicells synthesize a polypeptide (M(r) = 20,500) which is incorporated almost exclusively into the outer membrane of the minicell envelope. The gene (lom = lambda outer membrane) encoding this polypeptide has been mapped in the non-essential region of the lambda genome between coordinates 39.4% and 40.7% of lambda.
Mol Gen Genet 1979
PMID:Lambda encodes an outer membrane protein: the lom gene. 4 7

Bacillus subtilis RNA polymerase holoenzyme consists of the subunits beta', beta, sigma, alpha, delta, and omega. In sporulating bacteria and in bacteria infected with phages SP01 and SP82, this enzyme undergoes changes in subunit composition and transcriptional specificity that could play a regulatory role in gene transcription. Sporulating bacteria may contain a specific component that inhibits the activity of the sigma subunit of polymerase probably by interfering with the binding of sigma-polypeptide to core enzyme. The hypothetical inhibitor may be metabolically unstable, since its activity is rapidly depleted from sporulating cells in the presence of chloramphenicol. Inhibition of sigma-polypeptide activity may restrict the transcription of phage DNA an infected sporulating cells. Although lacking the sigma-subunit, RNA polymerase purified from sporulating cells contains sporulation-specific subunits of 85,000 and 27,000 daltons. In SP01-infected bacteria, the sigma-subunit is replaced by phage-induced subunits. Purified enzyme containing the protein product of SP01 regulatory gene 28 directs the transcription of phage middle genes in vitro, while enzyme containing phage-induced polypeptides V and VI preferentially copies late genes. Accurate transcription of middle and late genes in vitro requires the host delta-subunit of polymerase (or high ionic strength) but not sigma-subunit. Phage PBS2 induces an entirely new multisubunit RNA polymerase that specifically transcribes PBS2 DNA in vitro. This enzyme is synthesized de novo after infection and does not arise by modification of the B. subtilis holoenzyme.
Adv Enzymol Relat Areas Mol Biol 1976
PMID:Bacillus subtilis RNA polymerase and its modification in sporulating and phage-infected bacteria. 5 49

Ten out of 43 missense mutations in the lacZ gene of Escherchia coli gave rise to polypeptide chains that were degraded in vivo. While many of the mutants appeared to be fully or partially CRM-, there appeared to be no obvious correlation between degradation, map position, altered subunit association and the half-life of the mutant proteins.
Mol Gen Genet 1978 Aug 04
PMID:Degradation of missense mutant beta-galactosidase proteins in Escherichia coli K-12. 10 Jun 72

A set of mutants affected in translational fidelity was constructed by transduction within an otherwise isogenic Escherichia coli B argF40 argR11 background. Alterations in ribosomal proteins S4, S5, S12 and L6 either as single mutations or in various combinations were compared for their effects on aminoglycoside phenotypes, on in vivo and in vitro misreading and on the rate of peptide bond formation. Results may be summarized as follows: (i) Strains carrying two ambiguity mutations on the ribosome without any restrictive mutation are viable. When together, they only weakly increase the level of mistranslation as judged by several in vivo and in vitro test systems. (ii) The combination of two ram mutations causes a very strong cooperative increase of streptomycin sensitivity, irrespective of whether the strains have a wild-type S12 or mutationally altered S12 proteins (of the drug-resistant or -dependent types) on their ribosomes; (iii) The S4 and S5 ram mutations do not alter the response of the ribosome to aminoglycosides of the 2-desoxystreptamine group which are structurally unrelated to streptomycin. This is interpreted in terms of an effect of these ram mutations on the streptomycin binding site but not on the site(s) of binding of the other aminoglycosides. (iv) The rate of polypeptide bond formation which was determined from the kinetics of beta-galactosidase induction is not significantly changed in strains bearing the ram and the strA (streptomycin-resistant) alleles. In contrast, the L6 and the strA (streptomycin-dependent) alleles strongly reduce the rate of polypeptide elongation which mechanistically might be connected with restriction of ambiguity (Nino, 1974) in these cases.
Mol Gen Genet 1979 Mar 09
PMID:Bacterial ribosomes with two ambiguity mutations: effects of translational fidelity, on the response to aminoglycosides and on the rate of protein synthesis. 10 18

Specialized transducing phages lambda tna (tryptophanase) harboring chromosomal DNA and genetic markers from the dnaA region of the Escherichia coli chromosome were isolated. Transductional analysis showed that some of these tnaA transducing phages carry two genes important in DNA replication, namely the dnaA gene (initiation of chromosome replication) and the gyrB gene (subunit B of DNA gyrase), formerly designated couR. The following clockwise order of genetic markers was found: uhp, gyrB, dnaA, rimA, tnaA, bglB. The gene-protein relationship was established by the determination of the gene products encoded on the chromosomal DNA of the different lambda tna. A 54 kD and a 91 kD polypeptide appear to be coded for by the dnaA and gyrB genes, respectively; the 91 kD protein is encoded on a region in which coumermycin sensitivity maps and is with respect to electrophoretic behavior identical to subunit B of DNA gyrase. The 54 kD protein is encoded on the region in which different independently isolated dnaA(Ts) mutations (dnaA5, dnaA46, dnaA167, dnaA203, dnaA204, dnaA205, dnaA211, dnaA508) are located. Additional genes which code for polypeptides with hitherto unknown functions were identified and mapped. The acriflavin sensitivity mutation acrB1 was found to be an allele of the gyrB gene (see "Note Added in Proof").
Mol Gen Genet 1979 Sep
PMID:Characterization of the dnaA, gyrB and other genes in the dnaA region of the Escherichia coli chromosome on specialized transducing phages lambda tna. 16

Nuclear ribonucleoprotein (RNP) complexes that contain the U1 and U2 RNA of chromatin of Novikoff hepatoma cells were extracted with 0.01 M Tris-HCl (pH 8.0) after the nuclei were initially washed with 0.075 M NaCl and 0.025 M EDTA (pH 8.0). These RNP complexes were purified by chromatography on Sepharose 6B columns and centrifugation on sucrose density gradients. The identity of the U1 and U2 RNA in these particles was established by their electrophoretic mobility in polyacrylamide gels and their T1 RNase fingerprints which were identical with those of authentic U1 and U2 RNA (R. Reddy et al. (1974), J. Biol. Chem.249, 6486-6494; H. Shibata et al. (1974), Mol. Cell. Biochem. 4, 3-19). The nuclear riboncleoproteins had a buoyant density of 1.47 g/ml in CsCl gradients. Two-dimensional polyacrylamide gel electrophoresis of their proteins showed these RNP complexes contain 10 polypeptide spots, of which two are phosphorylated in vivo.
 ...
PMID:Nuclear ribonucleoprotein complexes containing U1 and U2 RNA. 16 94

Thr relevance of the crystal structure of the polypeptide hormones, insulin, glucagon and human placental lactogen to conformation and flexibility in solution and to receptor binding is considered. X-ray studies for crystal forms of glucagon, human placental lactogen and three insulin derivatives (A1 acetyl insulin, A1-t-butoxy carbonyl insulin and A1 2,2-dimethyl-3-formyl-L-thiazolidine-4-carbonyl insulin) are reported. Neither glucagon nor human placental lactogen are as ordered as insulin in the crystal form. Glucagon crystals undergo distinct transformations on changing the pH of the mother liquor from pH 9.5 to pH 6, indicating that the glucagon molecule is flexible in the crystal, as it is in solution. On the other hand all insulin analogues have a similar three dimensional structure to that of native insulin. Three dimensional difference Fourier studies of two insulin derivatives at 3 A resolution indicate the position of the modifying groups and define the small conformational changes which have occurred. The in vitro biological activity and receptor binding decrease with the increasing size of the group added to A1. The correlation of the structure analysis with the biological data strongly implicate a region close to A1 in receptor binding. Insulin appears to bind to the receptor in a specific conformation similar to that observed in the crystal structure and in solution; amino acid residues which are separated in the primary structure but brought into close juxtaposition in the tertiary structure are important for full potency.
Mol Cell Biochem 1975 Jul 31
PMID:The relation of polypeptide hormone structure and flexibility to receptor binding: the relevance of X-ray studies on insulins, glucagon and human placental lactogen. 17 May 5


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