Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:EXPT00572 (Asn)
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A herpes simplex virus type 2 (HSV-2) type-specific monoclonal antibody (MAb), CH-A9, precipitated a glycoprotein with an M(r) of approximately 30,000 (g30K) from extracts of HSV-2-infected BHK cells labelled with [3H]leucine, [14C]fructose or [3H]glucosamine. The M(r) of this glycoprotein is lower than those of other HSV glycoproteins. Immunoassays of BHK cells infected with HSV-1-HSV-2 intertypic recombinants localized the gene encoding the target antigen of MAb CH-A9 to the unique long (UL) region at map units 0.490 to 0.564. Tunicamycin effectively inhibits N-linked glycosylation of g30K, which suggests that g30K may be modified by addition of N-linked oligosaccharides and that the amino acid sequence may contain Asn-X-Ser or Asn-X-Thr. The g30K was also purified on an immunoadsorbent column consisting of MAb CH-A9 linked to Sepharose 4B and was shown to be an HSV-2 type-specific antigen by indirect ELISA. The glycoprotein could induce HSV-2 type-specific neutralizing antibody in BALB/c mice. This evidence suggests that g30K may be a novel glycoprotein of HSV-2.
J Gen Virol 1992 Jul
PMID:Identification and characterization of a 30K glycoprotein of herpes simplex virus type 2. 132 Dec 10

The amino acid sequence of the poliovirus 2C protein contains two highly conserved stretches, GSPGTGKS136 and MDD177, which correspond to the consensus 'A' and 'B' motifs (GXXXXGKS/T and DD/E, respectively) found in nucleoside triphosphate-binding proteins. To assess the functional importance of these amino acid sequences, we changed conserved and non-conserved amino acids. The replacement of the non-conserved Thr133 residue with Ser or Ala did not markedly change the virus phenotype. Similarly, replacement of the non-conserved Pro131 residue by Ala did not abolish virus viability, but changes of this residue to Thr or Asn were not tolerated. No viable mutant could be isolated after transfection of cultured cells with transcripts mutated at the conserved Lys135, Ser136 or Asp177 residues. However, true revertants were selected from Arg135 and Ser135 mutants, from Glu177 and Gly177 mutants, and from Ala136 mutants. Thr136 mutants not only gave rise to true revertants, but also to two independent isolates of a suppressor mutant, Asn140----Tyr. All the lethal mutations resulted in severe inhibition of viral RNA synthesis in vivo, although no translational deficiency was detected in a cell-free system. This is the first direct evidence for the functional significance of the nucleoside triphosphate-binding pattern in the poliovirus 2C protein.
J Gen Virol 1992 Aug
PMID:Analysis of the functional significance of amino acid residues in the putative NTP-binding pattern of the poliovirus 2C protein. 132 57

A bacteriocin produced by Pediococcus acidilactici has been purified to homogeneity by a rapid and simple four-step purification procedure which includes ammonium sulphate precipitation, chromatography with a cation-exchanger and Octyl Sepharose, and reverse-phase chromatography. The purification resulted in an approximately 80,000-fold increase in the specific activity and about a 6-fold increase in the total activity. The amino acid composition and sequencing data indicated that the bacteriocin contained 43-44 amino acid residues. The predicted M(r) and isolectric point of the bacteriocin are about 4600 and 8.6, respectively. Comparing the amino acid sequence of this bacteriocin with the sequences of leucocin A-UAL 187, sakacin P and curvacin A (bacteriocins produced by Leuconostoc gelidum, Lactobacillus sake and Lactobacillus curvatus, respectively) revealed that all four bacteriocins had in their N-terminal region the sequence Tyr-Gly-Asn-Gly-Val-Xaa-Cys, indicating that this concensus sequence is of fundamental importance for this group of bacteriocins. The bacteriocin from P. acidilactici and sakacin P were very similar, having at least 25 common amino acid residues. The sequence similarity was greatest in the N-terminal half of the molecules--17 of the first 19 residues were common--indicating the fundamental importance of this region. Leucocin A-UAL 187 and curvacin A had, respectively, at least 16 and 13 amino acid residues in common with the bacteriocin from P. acidilactici.
J Gen Microbiol 1992 Sep
PMID:Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. 140 95

The amino acid sequence of the bullfrog, Rana catesbeiana, follitropin beta-subunit has been determined by sequencing the intact protein (residues 1-39) and peptides originated by lysyl endopeptidase and pepsin. Twelve cysteine residues and two sugar chain binding sites at Asn-5 and Asn-22 are positional identities with bullfrog and mammalian beta-subunits. The bullfrog FSH beta-subunit is composed of 107 amino acid residues with a molecular mass of 11,782 Da, including the six cystine bridges and excepting the sugar chain. The bullfrog FSH beta-subunit has approximately 60% sequence identity with that of mammals and 40% with the fish gonadotropin beta-subunit. Conserved sequences among mammals (residue numbers 33-55 and 66-71) extensively differed from those of the bullfrog.
Gen Comp Endocrinol 1992 Oct
PMID:The complete amino acid sequence of the follitropin beta-subunit of the bullfrog, Rana catesbeiana. 142 58

Two hypertrehalosemic neuropeptides from the corpus cardiacum of the cockroach Polyphaga aegyptiaca were isolated by reversed-phase high-performance liquid chromatography, and their primary structures were determined by pulsed-liquid phase sequencing employing Edman chemistry, after enzymically deblocking the N-terminal pyroglutamate residue. As neither peptide was cleaved by carboxypeptidase, the C-terminus of each peptide was also blocked. Both peptides were found to be uncharged octapeptides with the sequences: Peptide 1: pGlu-Leu-Asn-Phe-Ser-Pro-Asn-Trp-NH2; and peptide 2: pGlu-Ile-Thr-Phe-Thr-Pro-Asn-Trp-NH2. Both peptides are clearly defined as members of the adipokinetic hormone/red pigment-concentrating hormone family of peptides. Whereas peptide 1 is identical in structure to the previously sequenced hypertrehalosemic neuropeptide from tenebrionid beetles (and is therefore designated the acronym Tem-HrTH), peptide 2 is a novel peptide and is designated the acronym Poa-HrTH. Both synthetic peptides caused an increase in the hemolymph carbohydrate concentration in P. aegyptiaca, specifically changing the trehalose concentration. The novel peptide Poa-HrTH was not very potent in elevating blood carbohydrates in the American cockroach.
Gen Comp Endocrinol 1992 Apr
PMID:Primary structures of the hypertrehalosemic peptides from corpora cardiaca of the primitive cockroach Polyphaga aegyptiaca. 150 21

Entomopoxviruses replicate in the cytoplasm of insect cells and characteristically produce occlusion bodies which serve to protect the virion from the environment; the major component of these bodies is a protein called spheroidin. We have previously identified and sequenced the gene encoding the major occlusion body protein of eastern spruce budworm (Choristoneura biennis) entomopoxvirus (CbEPV) and found it to encode a 47K polypeptide which aggregates due to the formation of intermolecular disulphide bonds. In this publication we demonstrate that the insect poxvirus of Amsacta moorei produces spheroidin with a unit Mr of 114.8K. The gene for this protein was cloned and sequenced, and the predicted polypeptide was demonstrated to contain 38 cysteine residues, a leucine zipper for possible protein-protein interactions and 14 potential Asn-linked glycosylation sites. Other than possessing a large number of sulphydryl groups, this protein showed no homology to its analogue found in cells infected with CbEPV. Antibodies directed against occlusion body proteins of the two viruses also failed to cross-react significantly on Western blots. In addition, nucleic acid probes prepared from the two different genes did not cross-hybridize on Southern blots of genomic DNA prepared from the viruses. Finally, the occlusion body proteins from the two insect viruses were compared with the A-type inclusion body protein of cowpox virus. Again, little homology between these proteins was evident, with the exception of a generally high cysteine content and a similarity between their late gene promoters. We conclude that the major occlusion body proteins of different poxviruses possess diverse primary structures, but all are capable of yielding large aggregates through the formation of disulphide bonds.
J Gen Virol 1992 Mar
PMID:The predicted amino acid sequence of the spheroidin protein from Amsacta moorei entomopoxvirus: lack of homology between major occlusion body proteins of different poxviruses. 154 19

The cell-wall-bound proteinase from Lactobacillus paracasei subsp. paracasei NCDO 151 was purified to homogeneity by anion-exchange and hydrophobic-interaction chromatography, chromatofocusing and gel-filtration. The purification resulted in a 600-700-fold increase in specific activity of the proteinase and the final yield was approximately 20%. Upon chromatofocusing, two proteolytically active components, termed pro135 and pro110, were detected. pro135 had an isoelectric point of 4.2. It had an Mr of about 300,000 as determined by gel-filtration and 135,000 as judged by SDS-PAGE, indicating that it may exist as a dimer in its native state. pro110 had an isoelectric point of 4.4, and an Mr of about 150,000 as determined by gel-filtration and 110,000 as judged by SDS-PAGE. pro110 appears to be a degradation product of pro135 as they have the same N-terminal amino acid sequence. The first N-terminal amino acid was ambiguous for both components, whereas the sequence from the second to the ninth amino acid was Ala-Lys-Ala-Asn-Ser-Met-Ala-Asn. This is identical to the corresponding sequence of the lactococcal cell-wall-bound proteinases. Although the Lactobacillus proteinase was a little smaller than the lactococcal proteinase, their purification characteristics were very similar, suggesting that these proteinases are related.
J Gen Microbiol 1992 Feb
PMID:Purification and N-terminal amino acid sequence determination of the cell-wall-bound proteinase from Lactobacillus paracasei subsp. paracasei. 156 42

Adrenocorticotropic (ACTH) and melanocyte stimulating (MSH) hormones have been demonstrated in the same cells in the cephalic half of the pars distalis of the chicken pituitary glands in three ways: (I) immunohistochemistry, (II) radioimmunoassay (RIA) using both anti-human or porcine ACTH and synthetic alpha-MSH antibodies, and (III) isolation and purification, followed by the determination of amino acid compositions of both hormones. The contents of ACTH and alpha-MSH are estimated by RIA to be 1600 and 10 ng/gland, respectively. ACTH missed 1 (des-Phe39-ACTH) or 2 residues (des-Glu38, Phe39-ACTH) from the C-terminal portion was also isolated. The recoveries of these ACTHs are differed from preparation to preparation. The complete amino acid sequence of chicken ACTH (39 residues) has been determined as NH2-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Arg-Lys-Arg- Arg- Pro-Ile-Lys-Val-Tyr-Pro-Asn-Gly-Val-Asp-Glu-Glu-Ser-Ala-Glu-Ser-Tyr-Pro- Met-Glu-Phe-OH Strikingly the amino acid sequence of chicken ACTH shows a closer resemblance to that from an amphibian, Xenopus (3 residue substitution) than that from another bird, the ostrich (7 residue substitution) or the turkey (at least 9 residue substitution).
Gen Comp Endocrinol 1991 Jun
PMID:Characterization of chicken ACTH and alpha-MSH: the primary sequence of chicken ACTH is more similar to Xenopus ACTH than to other avian ACTH. 165 32

The C-terminal region of human immunodeficiency virus (HIV) reverse transcriptase (RT) contains the domain responsible for RNase H activity. To determine the importance of this RNase H domain, specific changes in the C-terminal region of a recombinant RT expressed in Escherichia coli were introduced by amino acid substitutions and specific deletions. The enzyme activities of purified wild-type and mutant RT/RNase H proteins, standardized for protein content, were compared by filter assays and thermal inactivation kinetics. A point mutation of His 539----Asn produced an enzyme with a marked thermolabile RNase H function (nine-fold increase in inactivation), whereas RT function was only marginally more labile than that of the wild-type (two-fold). A second mutation, His 539----Asp, impaired both enzyme activities to a similar degree (four- to five-fold). A C-terminal deletion of 19 amino acids (aa) (aa 540 to 558) and a C-terminal truncation of 21 aa (aa 540 to 560) reduced RT as well as RNase H activity. A 130 aa deletion enzyme exhibited no RNase H activity and insufficient RT activity to allow inactivation studies. Two mutants, the 19 aa deletion and His----Asn, were introduced into proviral HIV-1 DNA clones to determine whether changes in enzyme activity, particularly RNase H activity, affected virus infectivity. Both mutants were non-infectious, indicating that the C-terminal 19 to 21 amino acids and His 539 of the RT/RNase H protein are essential for HIV replication. These results are consistent with the assumption that RNase H is essential for the infectivity of HIV-1.
J Gen Virol 1991 Jan
PMID:Mutations within the RNase H domain of human immunodeficiency virus type 1 reverse transcriptase abolish virus infectivity. 170 63

Pancreatic polypeptide (PP) has been purified from extracts of the pancreas of four species of odd-toed ungulates (Perissodactyla): Przewalski's horse, mountain zebra, white rhinoceros, and mountain tapir. The amino acid sequence of Przewalski's horse pancreatic polypeptide was established as Ala-Pro-Met-Glu-Pro-Val-Tyr-Pro-Gly-Asp10-Asn- Ala-Thr-Pro-Glu-Gln-Met-Ala-Gln-Tyr20-Ala-Ala-Glu-Leu-Arg-Arg-Tyr- Ile-Asn-Met30 - Leu-Thr-Arg-Pro-Arg-Tyr.NH2. Zebra PP was identical to Przewalski's horse PP, rhinoceros PP contained three substitutions relative to the horse (Ser for Ala1, Leu for Met3, and Glu for Gln16), and tapir PP contained one substitution relative to the horse (Leu for Met3). On the basis of morphological characteristics and the fossil record, the rhinocerotids are classified with the tapirids in the suborder Ceratomorpha, whereas the horse and zebra belong to a separate suborder, Hippomorpha. On the basis of structural similarity of the PP molecules, however, it would appear that the tapir is more closely related to the horse than to the rhinoceros. These observations provide a further example of the need for extreme caution when inferring taxonomic or phylogenetic relationships between species from the structures of homologous peptides.
Gen Comp Endocrinol 1991 Dec
PMID:Primary structure of pancreatic polypeptide from four species of Perissodactyla (Przewalski's horse, zebra, rhino, tapir). 180 25


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