scholarly journals Isolation and characterization of the chicken trypsinogen gene family

1995 ◽  
Vol 307 (2) ◽  
pp. 471-479 ◽  
Author(s):  
K Wang ◽  
L Gan ◽  
I Lee ◽  
L Hood
Keyword(s):  
Amino Acid ◽  
Gene Family ◽  
Amino Acid Level ◽  
Structural Features ◽  
Catalytic Triad ◽  
Amino Acid Residues ◽  
Isolation And Characterization ◽  
Anionic Trypsin ◽  
Cationic Trypsin

Based on genomic Southern hybridizations and cDNA sequence analyses, the chicken trypsinogen gene family can be divided into two multi-member subfamilies, a six-member trypsinogen I subfamily which encodes the cationic trypsin isoenzymes and a three-member trypsinogen II subfamily which encodes the anionic trypsin isoenzymes. The chicken cDNA and genomic clones containing these two subfamilies were isolated and characterized by DNA sequence analysis. The results indicated that the chicken trypsinogen genes encoded a signal peptide of 15 to 16 amino acid residues, an activation peptide of 9 to 10 residues and a trypsin of 223 amino acid residues. The chicken trypsinogens contain all the common catalytic and structural features for trypsins, including the catalytic triad His, Asp and Ser and the six disulphide bonds. The trypsinogen I and II subfamilies share approximately 70% sequence identity at the nucleotide and amino acid level. The sequence comparison among chicken trypsinogen subfamily members and trypsin sequences from other species suggested that the chicken trypsinogen genes may have evolved in coincidental or concerted fashion.

Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart

1991 ◽  
Vol 11 (1) ◽  
pp. 126-133 ◽  
Author(s):  
N Bacher ◽  
Y Zisman ◽  
E Berent ◽  
E Livneh
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Gene Family ◽  
Phorbol Esters ◽  
Structural Features ◽  
Cos Cells ◽  
Isolation And Characterization ◽  
Kinase C ◽  
Human Epidermoid Carcinoma

We have isolated and characterized a new human cDNA, coding for a protein kinase, related to the protein kinase C (PKC) gene family. Although this protein kinase shares some homologous sequences and structural features with the four members of the PKC family initially isolated (alpha, beta I, beta II, and gamma), it shows more homology with the recently described PKC-related subfamily, encoded by the cDNAs delta, epsilon, and zeta. The transcript for this gene product, termed PKC-L, is most abundant in lung tissue, less expressed in heart and skin tissue, and exhibited very low expression in brain tissue. Thus, its tissue distribution is different from that described for other mammalian members of the PKC gene family, their expression being enriched in brain tissues. PKC-L is also expressed in several human cell lines, including the human epidermoid carcinoma line A431. The ability of phorbol esters to bind to and stimulate the kinase activity of PKC-L was revealed by introducing the cDNA into COS cells.

scholarly journals The isolation and characterization of corticotropin from the pituitary gland of the ostrich Struthio camelus

1977 ◽  
Vol 165 (3) ◽  
pp. 519-523 ◽  
Author(s):  
R J Naudé ◽  
W Oelofsen
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Residues ◽  
Struthio Camelus ◽  
Isolation And Characterization ◽  
Isoelectric Points ◽  
Pituitary Glands ◽  
Amide Content

1. Avian corticotropin (ACTH) was purified from both fresh and aged pituitary glands of the ostrich Struthio camelus. 2. The isolation of corticotropin in pure form involved acid/acetone extraction, NaCl fractionation, CM-cellulose chromatography and Sephadex G-50 chromatography. 3. The hormone preparations from fresh and aged glands behaved as single substances on polyacrylamide-gel electrophoresis, and both preparations were found to consist of 39 amino acid residues, in identical molar proportions for the different amino acids. 4. The isoelectric points of the two hormone preparations were estimated to be in the range pH 8.3-8.7, indicating possible differences in amide content, and the N-terminal amino acid of both preparations appeared to be serine. 5. The hormone preparations from fresh and aged glands exhibited similar biological potencies (73 and 77 i.u./mg respectively), as measured by steroidogenesis in vitro. 6. Apart from possible differences in amide content, the corticotropin preparations obtained from fresh and aged glands appear to be indistinguishable.

scholarly journals Isolation and Characterization of a Novel Cold-Active, Halotolerant Endoxylanase from Echinicola rosea Sp. Nov. JL3085T

Marine Drugs ◽  
2020 ◽  
Vol 18 (5) ◽  
pp. 245
Author(s):  
Jianlong He ◽  
Le Liu ◽  
Xiaoyan Liu ◽  
Kai Tang
Keyword(s):  
Amino Acid ◽  
Marine Bacterium ◽  
Maximum Velocity ◽  
Maximum Activity ◽  
Glycoside Hydrolases ◽  
Amino Acid Residues ◽  
Xylanase Gene ◽  
Isolation And Characterization ◽  
Cold Active

We cloned a xylanase gene (xynT) from marine bacterium Echinicola rosea sp. nov. JL3085T and recombinantly expressed it in Escherichia coli BL21. This gene encoded a polypeptide with 379 amino acid residues and a molecular weight of ~43 kDa. Its amino acid sequence shared 45.3% similarity with an endoxylanase from Cellvibrio mixtus that belongs to glycoside hydrolases family 10 (GH10). The XynT showed maximum activity at 40 °C and pH 7.0, and a maximum velocity of 62 μmoL min−1 mg−1. The XynT retained its maximum activity by more than 69%, 51%, and 26% at 10 °C, 5 °C, and 0 °C, respectively. It also exhibited the highest activity of 135% in the presence of 4 M NaCl and retained 76% of its activity after 24 h incubation with 4 M NaCl. This novel xylanase, XynT, is a cold-active and halotolerant enzyme that may have promising applications in drug, food, feed, and bioremediation industries.

scholarly journals Isolation and characterization of phosphorylated bovine prolactin

1993 ◽  
Vol 296 (1) ◽  
pp. 41-47 ◽  
Author(s):  
B G Kim ◽  
C L Brooks
Keyword(s):  
Amino Acid ◽  
Phosphorylation Site ◽  
Growth Hormones ◽  
Amino Acid Residues ◽  
Placental Lactogens ◽  
Structural Conformation ◽  
Isolation And Characterization ◽  
Sequencing Studies ◽  
Phosphorylated Prolactin

Quantitative isolation of bovine prolactin was accomplished by immunoaffinity chromatography using clonal antibody as the stationary ligand. The phosphorylated and non-phosphorylated (native) prolactins contained in the immunopurified preparations were separated by chromatofocusing. Isolates from individual pituitaries revealed that phosphorylated prolactin represented between 20 and 80% of the total prolactin. The stoichiometry of phosphate in phosphorylated prolactin was 1.4:1 when determined by amino acid analysis after preparation of the S-ethylcysteine derivative. One major phosphorylation site, serine-90, and two minor sites, serine-26 and -34, were determined by mapping and sequencing studies. Serine-90 was conserved in prolactins, growth hormones and placental lactogens. Serine-26 and -34 were conserved in prolactins, but were not found in growth hormones or placental lactogens. Absorption spectroscopy of the aromatic amino acid residues indicated that phosphorylation of prolactin was associated with a unique structural conformation.

scholarly journals Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart.

1991 ◽  
Vol 11 (1) ◽  
pp. 126-133 ◽  
Author(s):  
N Bacher ◽  
Y Zisman ◽  
E Berent ◽  
E Livneh
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Gene Family ◽  
Phorbol Esters ◽  
Structural Features ◽  
Cos Cells ◽  
Isolation And Characterization ◽  
Kinase C ◽  
Human Epidermoid Carcinoma

We have isolated and characterized a new human cDNA, coding for a protein kinase, related to the protein kinase C (PKC) gene family. Although this protein kinase shares some homologous sequences and structural features with the four members of the PKC family initially isolated (alpha, beta I, beta II, and gamma), it shows more homology with the recently described PKC-related subfamily, encoded by the cDNAs delta, epsilon, and zeta. The transcript for this gene product, termed PKC-L, is most abundant in lung tissue, less expressed in heart and skin tissue, and exhibited very low expression in brain tissue. Thus, its tissue distribution is different from that described for other mammalian members of the PKC gene family, their expression being enriched in brain tissues. PKC-L is also expressed in several human cell lines, including the human epidermoid carcinoma line A431. The ability of phorbol esters to bind to and stimulate the kinase activity of PKC-L was revealed by introducing the cDNA into COS cells.

scholarly journals Isolation and Characterization of a Hantavirus from Lemmus sibiricus: Evidence for Host Switch during Hantavirus Evolution

1999 ◽  
Vol 73 (7) ◽  
pp. 5586-5592 ◽  
Author(s):  
Olli Vapalahti ◽  
Åke Lundkvist ◽  
Vadim Fedorov ◽  
Christopher J. Conroy ◽  
Sirpa Hirvonen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Level ◽  
Amino Acid Identity ◽  
Rodent Host ◽  
Host Switch ◽  
Acid Identity ◽  
Noncoding Regions ◽  
Isolation And Characterization ◽  
Focus Reduction

ABSTRACT A novel hantavirus, first detected in Siberian lemmings (Lemmus sibiricus) collected near the Topografov River in the Taymyr Peninsula, Siberia (A. Plyusnin et al., Lancet 347:1835–1836, 1996), was isolated in Vero E6 cells and in laboratory-bred Norwegian lemmings (Lemmus lemmus). The virus, named Topografov virus (TOP), was most closely related to Khabarovsk virus (KBR) and Puumala viruses (PUU). In a cross focus reduction neutralization test, anti-TOP Lemmus antisera showed titers at least fourfold higher with TOP than with other hantaviruses; however, a rabbit anti-KBR antiserum neutralized TOP and KBR at the same titer. The TOP M segment showed 77% nucleotide and 88% amino acid identity with KBR and 76% nucleotide and 82% amino acid identity with PUU. However, the homology between TOP and the KBR S segment was disproportionately higher: 88% at the nucleotide level and 96% at the amino acid level. The 3′ noncoding regions of KBR and the TOP S and M segments were alignable except for 113- and 58-nucleotide deletions in KBR. The phylogenetic relationships of TOP, KBR, and PUU and their respective rodent carriers suggest that an exceptional host switch took place during the evolution of these viruses; while TOP and KBR are monophyletic, the respective rodent host species are only distantly related.

scholarly journals Isolation and Characterization Of Rice R Genes: Evidence for Distinct Evolutionary Paths in Rice and Maize

Genetics ◽  
1996 ◽  
Vol 142 (3) ◽  
pp. 1021-1031 ◽  
Author(s):  
Jianping Hu ◽  
Beth Anderson ◽  
Susan R Wessler
Keyword(s):  
Gene Family ◽  
Gene Families ◽  
Chromosome 1 ◽  
R Gene ◽  
R Genes ◽  
Helix Loop Helix ◽  
Isolation And Characterization ◽  
Undetermined Function ◽  
Evolutionary Paths

Abstract R and B genes and their homologues encode basic helix-loop-helix (bHLH) transcriptional activators that regulate the anthocyanin biosynthetic pathway in flowering plants. In maize, R/B genes comprise a very small gene family whose organization reflects the unique evolutionary history and genome architecture of maize. To know whether the organization of the R gene family could provide information about the origins of the distantly related grass rice, we characterized members of the R gene family from rice Oryza sativa. Despite being a true diploid, O. sativa has at least two R genes. An active homologue (Ra) with extensive homology with other R genes is located at a position on chromosome 4 previously shown to be in synteny with regions of maize chromosomes 2 and 10 that contain the B and R loci, respectively. A second rice R gene (Rb) of undetermined function was identified on chromosome 1 and found to be present only in rice species with AA genomes. All non-AA species have but one R gene that is Ra-like. These data suggest that the common ancestor shared by maize and rice had a single R gene and that the small R gene families of grasses have arisen recently and independently.

scholarly journals Isolation and Characterization of Rat Cytochrome P-450IIB Gene Family Members

1989 ◽  
Vol 264 (12) ◽  
pp. 7046-7053 ◽  
Author(s):  
C M Giachelli ◽  
J Lin-Jones ◽  
C J Omiecinski
Keyword(s):  
Gene Family ◽  
Family Members ◽  
Isolation And Characterization
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