Cloning and characterization of the cDNA encoding the PH20 protein in the European red fox Vulpes vulpes

1998 ◽  
Vol 10 (2) ◽  
pp. 165 ◽  
Author(s):  
José ten Have ◽  
Sandra Beaton ◽  
Mark P. Bradley
Keyword(s):  
Transmembrane Domain ◽  
Red Fox ◽  
Accession Number ◽  
C Terminus ◽  
Acrosomal Membrane ◽  
Testis Cdna Library ◽  
Testis Cdna ◽  
Mammalian Fertilization ◽  
Inner Acrosomal Membrane

The PH20 protein is thought to play a crucial role in mammalian fertilization. The fox PH20homologue has been cloned from a testis cDNA library and the deduced protein sequence shows high levels of homology to PH20 proteins isolated from other species. Unlike other PH20 proteins the fox protein does not appear to be membrane associated through a GPI-linkage nor does it show the presence of a transmembrane domain at the C-terminus of the protein. It is in this region that the proteins appear to be least conserved. Immunolocalization studies on fox sperm show that the PH20 protein is located on the inner acrosomal membrane. Transcription of PH20 in the fox is seasonally regulated, with the mRNA expressed during those months when spermatogenesis is at its peak. The PH20 sequence described in this paper has been submitted to the Genbank database and has the accession number U41412.

Identification and characterization of a gene coding a novel isoform of DEAD-box protein

2002 ◽  
Vol 14 (3) ◽  
pp. 185 ◽  
Author(s):  
Lanlan Yin ◽  
JianMin Li ◽  
Hu Zhu ◽  
Min Lin ◽  
Lijun Cheng ◽  
...  
Keyword(s):  
Human Testis ◽  
Microarray Hybridization ◽  
Chain Reaction ◽  
Dead Box ◽  
Gene Coding ◽  
Testis Cdna Library ◽  
Testis Cdna ◽  
Polymerase Chain ◽  
Identification And Characterization

A gene coding a novel isoform of DEAD-box protein named testicular DEAD-box protein (tDbp), presumably involved in testicular function, was identified and characterized. Testicular DEAD-box protein was cloned from a human testis cDNA library. The cDNA microarray hybridization showed that it was expressed at a higher level in adult testis than in embryo testis. Reverse transcription-polymerase chain reaction indicated that tDbp was specifically expressed in testis, but not in some other tissues.

Cloning, sequencing, and characterization of LDH-C4 from a fox testis cDNA library

1996 ◽  
Vol 44 (4) ◽  
pp. 452-459 ◽  
Author(s):  
Mark P. Bradley ◽  
Amber Geelan ◽  
Virginia Leitch ◽  
Erwin Goldberg
Keyword(s):  
Cdna Library ◽  
Testis Cdna Library ◽  
Testis Cdna

scholarly journals Characterization of a UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase with an unusual lectin domain from the platyhelminth parasite Echinococcus granulosus

2004 ◽  
Vol 382 (2) ◽  
pp. 501-510 ◽  
Author(s):  
Teresa FREIRE ◽  
Cecilia FERNÁNDEZ ◽  
Cora CHALAR ◽  
Rick M. MAIZELS ◽  
Pedro ALZARI ◽  
...  
Keyword(s):  
Echinococcus Granulosus ◽  
Transmembrane Domain ◽  
Functional Characterization ◽  
Maximal Activity ◽  
Structural Features ◽  
Helminth Parasites ◽  
Lectin Domain ◽  
C Terminus ◽  
The One

As part of a general project aimed at elucidating the initiation of mucin-type O-glycosylation in helminth parasites, we have characterized a novel ppGalNAc-T (UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase) from the cestode Echinococcus granulosus (Eg-ppGalNAc-T1). A full-length cDNA was isolated from a library of the tissue-dwelling larval stage of the parasite, and found to code for a 654-amino-acid protein containing all the structural features of ppGalNAc-Ts. Functional characterization of a recombinant protein lacking the transmembrane domain showed maximal activity at 28 °C, in the range 6.5–7.5 pH units and in the presence of Cu2+. In addition, it transferred GalNAc to a broad range of substrate peptides, derived from human mucins and O-glycosylated parasite proteins, including acceptors containing only serine or only threonine residues. Interestingly, the C-terminal region of Eg-ppGalNAc-T1 bears a highly unusual lectin domain, considerably longer than the one from other members of the family, and including only one of the three ricin B repeats generally present in ppGalNAc-Ts. Furthermore, a search for conserved domains within the protein C-terminus identified a fragment showing similarity to a recently defined domain, specialized in the binding of organic phosphates (CYTH). The role of the lectin domain in the determination of the substrate specificity of these enzymes suggests that Eg-ppGalNAc-T1 would be involved in the glycosylation of a special type of substrate. Analysis of the tissue distribution by in situ hybridization and immunohistochemistry revealed that this transferase is expressed in the hydatid cyst wall and the subtegumental region of larval worms. Therefore it could participate in the biosynthesis of O-glycosylated parasite proteins exposed at the interface between E. granulosus and its hosts.

scholarly journals Screening a Strain of Klebsiella sp. O852 and the Optimization of Fermentation Conditions for Trans-Dihydrocarvone Production

Molecules ◽  
2021 ◽  
Vol 26 (9) ◽  
pp. 2432
Author(s):  
Li Chen ◽  
Lu-Lu Zhang ◽  
Jing-Nan Ren ◽  
Xiao Li ◽  
Gang Fan ◽  
...  
Keyword(s):  
Ethanol Concentration ◽  
Flavor Compounds ◽  
Accession Number ◽  
Reaction Parameters ◽  
Isolation And Characterization ◽  
Biotransformation Process ◽  
Pharmaceutical Industries ◽  
Final Ethanol Concentration ◽  
Optimization Of Fermentation

Flavors and fragrances have high commercial value in the food, cosmetic, chemical and pharmaceutical industries. It is interesting to investigate the isolation and characterization of new microorganisms with the ability to produce flavor compounds. In this study, a new strain of Klebsiella sp. O852 (accession number CCTCC M2020509) was isolated from decayed navel orange (Citrus sinensis (L.) Osbeck), which was proved to be capable of converting limonene to trans-dihydrocarvone. Besides, the optimization of various reaction parameters to enhance the trans-dihydrocarvone production in shake flask was performed for Klebsiella sp. O852. The results showed that the yield of trans-dihydrocarvone reached up to 1 058 mg/L when Klebsiella sp. O852 was incubated using LB-M medium for 4 h at 36 °C and 150 rpm, and the biotransformation process was monitored for 36 h after adding 1680 mg/L limonene/ethanol (final ethanol concentration of 0.8% (v/v)). The content of trans-dihydrocarvone increased 16 times after optimization. This study provided a basis and reference for producing trans-dihydrocarvone by biotransformation.

scholarly journals Characterization of an activated human ros gene.

1986 ◽  
Vol 6 (9) ◽  
pp. 3109-3116 ◽  
Author(s):  
C Birchmeier ◽  
D Birnbaum ◽  
G Waitches ◽  
O Fasano ◽  
M Wigler
Keyword(s):  
Gene Transfer ◽  
Protein Kinases ◽  
Transmembrane Domain ◽  
Extracellular Domain ◽  
Kinase Domain ◽  
Specific Protein ◽  
Normal Human

A human oncogene, mcf3, previously detected by a combination of DNA-mediated gene transfer and a tumorigenicity assay, derives from a human homology of the avian v-ros oncogene. Both v-ros and mcf3 can encode a protein with homology to tyrosine-specific protein kinases, and both mcf3 and v-ros encode a potential transmembrane domain N terminal to the kinase domain. mcf3 probably arose during gene transfer from a normal human ros gene by the loss of a putative extracellular domain. There do not appear to be any other gross rearrangements in the structure of mcf3.

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