scholarly journals Cloning of a galactose-binding lectin from the venom of Trimeresurus stejnegeri

1999 ◽  
Vol 341 (3) ◽  
pp. 733-737 ◽  
Author(s):  
Qiang XU ◽  
Xiang-Fu WU ◽  
Qi-Chang XIA ◽  
Ke-Yi WANG
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Snake Venom ◽  
Coding Region ◽  
Amino Acid Signal Peptide ◽  
On Line ◽  
Cloned Cdna ◽  
Binding Lectin ◽  
Amino Acid Signal ◽  
Galactose Binding Lectin

A galactose-binding lectin isolated from the venom of Trimeresurus stejnegeri is a homodimer C-type lectin. The cloned cDNA encoding the monomer of Trimeresurus stejnegerilectin (TSL) was sequenced and found to contain a 5′-end non-coding region, a sequence which encodes 135 amino acids, including a typical 23 amino acid signal peptide followed by the mature protein sequence, a 3′-end non-coding region, a polyadenylation signal, and a poly(A) region. To completely characterize the deduced amino acid sequence, on-line HPLC-MS and tandem MS were used to analyse the intact monomer and its proteolytic peptides. A modified peptide fragment was also putatively identified by HPLC-MS analysis. The deduced amino acid sequence was found to contain a carbohydrate-recognition domain homologous with those of some known C-type animal lectins. Thus TSL belongs to group VII of the C-type animal lectins as classified by Drickamer [(1993) Prog. Nucleic Acid Res. Mol. Biol. 45, 207-232]. At present, a number of C-type lectins have been purified from snake venom, but most of them have been characterized only at the protein level. To our knowledge, this is the first known cDNA sequence of a true C-type lectin from snake venom.

Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA

1987 ◽  
Vol 143 (2) ◽  
pp. 740-748 ◽  
Author(s):  
Micheline Misrahi ◽  
Michel Atger ◽  
Luc d'Auriol ◽  
Hugues Loosfelt ◽  
Cécile Meriel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Progesterone Receptor ◽  
Amino Acid Sequence ◽  
Complete Amino Acid Sequence ◽  
Cloned Cdna ◽  
Human Progesterone Receptor

scholarly journals Nucleotide and derived amino acid sequences of a cDNA coding for pre-uteroglobin from the lung of the hare (Lepus capensis)

1986 ◽  
Vol 235 (3) ◽  
pp. 895-898 ◽  
Author(s):  
M S López de Haro ◽  
A Nieto
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Untranslated Regions ◽  
Coding Region ◽  
Homologous Proteins ◽  
Lepus Capensis ◽  
Rabbit Gene

An almost full-length cDNA coding for pre-uteroglobin from hare lung was cloned and sequenced. The derived amino acid sequence indicated that hare pre-uteroglobin contained 91 amino acids, including a signal peptide of 21 residues. Comparison of the nucleotide sequence of hare pre-uteroglobin cDNA with that previously reported for the rabbit gene indicated five silent point substitutions and six others leading to amino acid changes in the coding region. The untranslated regions of both pre-uteroglobin mRNAs were very similar. The amino acid changes observed are discussed in relation to the different progesterone-binding abilities of both homologous proteins.

scholarly journals Identification and expression of Pen c 2, a novel allergen from Penicillium citrinum

1999 ◽  
Vol 341 (1) ◽  
pp. 51-59 ◽  
Author(s):  
Lu-Ping CHOW ◽  
Ning-Yuan SU ◽  
Chia-Jung YU ◽  
Bor-Luen CHIANG ◽  
Horng-Der SHEN
Keyword(s):  
Amino Acid ◽  
Serine Proteases ◽  
Catalytic Triad ◽  
Penicillium Citrinum ◽  
E Coli ◽  
Acid Protein ◽  
Amino Acid Signal Peptide ◽  
Cloned Cdna ◽  
Allergic Disorders ◽  
Amino Acid Protein

The mould genus, Penicillium, is known to be a significant source of environmental aero-allergens. One important allergen from Penicillium citrinum, Pen c 2, has been identified by means of two-dimensional immunoblotting using IgE-containing patients' sera. This novel allergen was cloned, sequenced and expressed in Escherichia coli. The cloned cDNA encodes a large 457-amino acid protein precursor containing a 16-amino acid signal peptide, a 120-amino acid propeptide and the 321-amino acid mature protein. Comparison of the Pen c 2 sequence with known protein sequences revealed shared high sequence similarities with two vacuolar serine proteases from Aspergillus niger and Saccharomyces cerevisiae. Asp-46, His-78 and Ser-244 were found to constitute the catalytic triad of the 39-kDa Pen c 2. The DNA coding for Pen c 2 was cloned into vector PQE-30 and expressed in E. coli as a His-tag fusion protein that bound serum IgE from Penicillium-allergic patients on immunoblots. Recombinant Pen c 2 could therefore be used effectively for diagnosis and also potentially for the treatment of mould-derived allergic disorders.

scholarly journals Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and localization of the gene to chromosome 17

Blood ◽  
1988 ◽  
Vol 72 (2) ◽  
pp. 593-600 ◽  
Author(s):  
JP Rosa ◽  
PF Bray ◽  
O Gayet ◽  
GI Johnston ◽  
RG Cook ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Chromosome 17 ◽  
Coding Region ◽  
Membrane Glycoproteins ◽  
Cdna Sequences ◽  
Hel Cells ◽  
Adhesive Proteins

Abstract Platelet aggregation requires the binding of adhesive proteins such as fibrinogen to the heterodimer of membrane glycoproteins IIb (GPIIb) and IIIa (GPIIIa). Human erythroleukemia (HEL) cells synthesize both GPIIb and GPIIIa. Using poly(A+) RNA purified from HEL cells, we constructed a cDNA library in the lambda gt10 phage vector. This library was screened with a 38mer oligonucleotide derived from a platelet GPIIIa peptide, and three overlapping cDNAs were isolated. The three inserts encompassed 3.5 kilobases (kb), including the entire coding region of mature GPIIIa (2,286 basepairs, bp) and 1.3 kb of 3′ untranslated sequence. All 222 residues determined directly from platelet GPIIIa tryptic peptides exactly matched the HEL cell-deduced amino acid sequence. The HEL cell sequence matched a previously reported endothelial cell cDNA sequence except for eight nucleotides. Five of these nucleotide differences were silent changes consistent with genetic polymorphisms. The other three differences resulted in changes in the deduced amino acid sequence of GPIIIa; reexamination of the endothelial cell cDNA sequence in these three areas revealed that it is actually identical to the HEL cell sequence. The virtual identity of the endothelial and HEL cell cDNA sequences provides direct evidence that GPIIIa is a subunit common to cell-adhesion receptors present in more than one cell type. We localized the gene for GPIIIa to chromosome 17, the same chromosome to which we had previously mapped the gene for GPIIb.

Amino acid sequence of a snake venom toxin that binds to the muscarinic acetylcholine receptor

Toxicon ◽  
1991 ◽  
Vol 29 (4-5) ◽  
pp. 521-526 ◽  
Author(s):  
Evert Karlsson ◽  
Carl Risinger ◽  
Mikael Jolkkonen ◽  
Christer Wernstedt ◽  
Abdu Adem
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acetylcholine Receptor ◽  
Snake Venom ◽  
Muscarinic Acetylcholine Receptor ◽  
Muscarinic Acetylcholine ◽  
Venom Toxin ◽  
Snake Venom Toxin
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