scholarly journals The sequence of the mouse 14 kDa β-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes

1989 ◽  
Vol 261 (3) ◽  
pp. 847-852 ◽  
Author(s):  
T J G Wilson ◽  
M N Firth ◽  
J T Powell ◽  
F L Harrison
Keyword(s):  
Amino Acid ◽  
Basement Membrane ◽  
Amino Acid Sequence ◽  
Genomic Dna ◽  
Cdna Probe ◽  
Cdna Clones ◽  
Partial Amino Acid Sequence ◽  
3T3 Fibroblasts ◽  
Cytoplasmic Ribosomes ◽  
Binding Lectin

The partial amino acid sequence of the mouse 14 kDa beta-galactoside-binding lectin has been deduced from cDNA clones corresponding to 86% of the coding sequence and extending to the polyadenylation signal. The deduced amino acid sequence for the murine lectin shows 94% identity with the rat, 89% with human, 86% with bovine and 46% with the chicken 14 kDa lectins. A cDNA probe has been used to analyse genomic DNA and identify a single mRNA of approx. 570 bp in 3T3 fibroblasts, murine erythroleukaemia cells and the murine basement-membrane-secreting Engelbreth-Holm-Swarm tumour. Analysis of free and bound polyribosomes has shown that the lectin message is translated on free cytoplasmic ribosomes.

Molecular studies on osmoprimed seeds of cauliflower: a partial amino acid sequence of a vigour-related protein and osmopriming-enhanced expression of putative aspartic protease

1995 ◽  
Vol 5 (3) ◽  
pp. 177-181 ◽  
Author(s):  
Yuzo Fujikura ◽  
Cees M. Karssen
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Probe ◽  
Soybean Seed ◽  
Aspartic Protease ◽  
Cdna Clones ◽  
High Homology ◽  
Related Protein ◽  
Partial Amino Acid Sequence ◽  
Two Dimensional Gel Electrophoresis

AbstractA partial amino acid sequence of a vigour-related protein, V-1, from cauliflower (Brassica oleracea L.) seeds was obtained, after isolation by two-dimensional gel electrophoresis and gas-phase micro-sequencing. The sequence was found to have high homology to soybean seed maturation proteins. However, the position of the sequence in the V-1 polypeptide suggests that the V-1 and soybean proteins have different polypeptide structures. An osmoprimed seeds cDNA library was constructed and has been screened by a cDNA probe derived from the V-1 sequence. Two cDNA clones with high homology to aspartic protease (EC 3.4.23) from barley grain were isolated. The expression of putative aspartic protease mRNA was found to be enhanced by osmopriming, however the clones were found to have no significant sequence homology to the V-1.

Partial amino acid sequence of human thrombospondin as determined by analysis of cDNA clones: homology to malarial circumsporozoite proteins

Biochemistry ◽  
1986 ◽  
Vol 25 (26) ◽  
pp. 8418-8425 ◽  
Author(s):  
Sentaro Kobayashi ◽  
Francine Eden-McCutchan ◽  
Paul Framson ◽  
Paul Bornstein
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Clones ◽  
Partial Amino Acid Sequence

scholarly journals Evidence that the 14 kDa soluble β-galactoside-binding lectin in man is encoded by a single gene

1989 ◽  
Vol 259 (1) ◽  
pp. 291-294 ◽  
Author(s):  
W M Abbott ◽  
T Feizi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Cell ◽  
Cdna Clone ◽  
Human Placenta ◽  
Southern Blotting ◽  
Single Gene ◽  
Cdna Probe ◽  
Human Cell Lines ◽  
Binding Lectin

A full-length cDNA clone for the 14 kDa soluble beta-galactoside-binding lectin of man has been isolated from a cDNA library from HepG2 hepatoma cells. The derived amino acid sequence is identical with that of the 14 kDa lectin from human placenta. The results of Northern and Southern blotting of several different human cell lines using a cDNA probe for the 14 kDa lectin suggest the presence of a single gene for this protein. Thus, although there are multiple proteins in the range 14-200 kDa which are antigenically related to this lectin, we would conclude from the present study that there is only one gene for the 14 kDa lectin.

scholarly journals Soluble bovine galactose-binding lectin. cDNA cloning reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein

1989 ◽  
Vol 259 (1) ◽  
pp. 283-290 ◽  
Author(s):  
W M Abbott ◽  
A Mellor ◽  
Y Edwards ◽  
T Feizi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Cdna Library ◽  
Basic Protein ◽  
Cdna Clones ◽  
Antigenic Relationship ◽  
Lectin Protein ◽  
Binding Lectin ◽  
Major Domain

A full-length cDNA clone for the 13-14 kDa soluble beta-galactoside-binding lectin was isolated from a bovine fibroblast cDNA library. The derived amino acid sequence shows eight differences from a preliminary partial amino acid sequence given previously for the bovine heart lectin. This observation led to a re-examination of the data and correction of the heart lectin protein sequence. Except for a possible polymorphism of the heart lectin at position 57, the fibroblast and heart lectin sequences are considered identical. The epitope recognized by two monoclonal anti-(bovine lectin) antibodies, 36/8 and 9/5, was identified as the tetrapeptide sequence W-G-A/S-E/D by the isolation of several different cDNA clones from a human intestine cDNA library. A similar tetrapeptide is present in all of the soluble beta-galactoside-binding animal lectins sequenced thus far. It is also found in myelin basic protein, which we show is antigenically cross-reactive with the lectin. In myelin basic protein the tetrapeptide is a part of the major domain previously shown to be responsible for the induction of experimental allergic encephalomyelitis.

GLI3 encodes a 190-kilodalton protein with multiple regions of GLI similarity

1990 ◽  
Vol 10 (10) ◽  
pp. 5408-5415
Author(s):  
J M Ruppert ◽  
B Vogelstein ◽  
K Arheden ◽  
K W Kinzler
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Amino Acid Sequence ◽  
Zinc Finger ◽  
Sequence Comparison ◽  
Genomic Dna ◽  
Zinc Fingers ◽  
Cdna Clones ◽  
Target Sequence ◽  
Amino Acid Sequence Comparison

The GLI oncogene, discovered by virtue of its amplification in human tumors, encodes a sequence-specific DNA-binding protein containing five zinc fingers. We have now characterized one member of a family of GLI-related zinc finger genes. A previously identified fragment of GLI3 genomic DNA was used to localize GLI3 to chromosome 7p13 and to isolate cDNA clones. Sequence analysis of these clones and identification of the GLI3 protein by using polyclonal antisera demonstrated that GLI3 encodes a protein of 1,596 amino acids and an apparent molecular mass of 190 kilodaltons. Amino acid sequence comparison with GLI demonstrated seven regions of similarity (53 to 88% identity), with the zinc fingers representing the most similar region. Furthermore, when produced in vitro, the GLI3 protein bound specifically to genomic DNA fragments containing GLI-binding sites. Amino acid sequence comparison with the product of another member of the GLI family, the Drosophila segment polarity gene cubitus interruptus Dominant, revealed additional similarity that was not shared with GLI. These studies suggest that the GLI-related genes encode a family of DNA-binding proteins with related target sequence specificities. In addition, sequence similarity aside from the zinc finger region suggests that other aspects of function are shared among the members of this gene family.

scholarly journals GLI3 encodes a 190-kilodalton protein with multiple regions of GLI similarity.

1990 ◽  
Vol 10 (10) ◽  
pp. 5408-5415 ◽  
Author(s):  
J M Ruppert ◽  
B Vogelstein ◽  
K Arheden ◽  
K W Kinzler
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Amino Acid Sequence ◽  
Zinc Finger ◽  
Sequence Comparison ◽  
Genomic Dna ◽  
Zinc Fingers ◽  
Cdna Clones ◽  
Target Sequence ◽  
Amino Acid Sequence Comparison

The GLI oncogene, discovered by virtue of its amplification in human tumors, encodes a sequence-specific DNA-binding protein containing five zinc fingers. We have now characterized one member of a family of GLI-related zinc finger genes. A previously identified fragment of GLI3 genomic DNA was used to localize GLI3 to chromosome 7p13 and to isolate cDNA clones. Sequence analysis of these clones and identification of the GLI3 protein by using polyclonal antisera demonstrated that GLI3 encodes a protein of 1,596 amino acids and an apparent molecular mass of 190 kilodaltons. Amino acid sequence comparison with GLI demonstrated seven regions of similarity (53 to 88% identity), with the zinc fingers representing the most similar region. Furthermore, when produced in vitro, the GLI3 protein bound specifically to genomic DNA fragments containing GLI-binding sites. Amino acid sequence comparison with the product of another member of the GLI family, the Drosophila segment polarity gene cubitus interruptus Dominant, revealed additional similarity that was not shared with GLI. These studies suggest that the GLI-related genes encode a family of DNA-binding proteins with related target sequence specificities. In addition, sequence similarity aside from the zinc finger region suggests that other aspects of function are shared among the members of this gene family.

scholarly journals The murine Fc receptor for immunoglobulin: purification, partial amino acid sequence, and isolation of cDNA clones.

1986 ◽  
Vol 83 (18) ◽  
pp. 6980-6984 ◽  
Author(s):  
M. L. Hibbs ◽  
I. D. Walker ◽  
L. Kirszbaum ◽  
G. A. Pietersz ◽  
N. J. Deacon ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Fc Receptor ◽  
Cdna Clones ◽  
Partial Amino Acid Sequence

Paris I Dysfibrinogenemia: A Point Mutation in Intron 8 Results in Insertion of a 15 Amino Acid Sequence in the Fibrinogen γ-Chain

1993 ◽  
Vol 69 (03) ◽  
pp. 217-220 ◽  
Author(s):  
Jonathan B Rosenberg ◽  
Peter J Newman ◽  
Michael W Mosesson ◽  
Marie-Claude Guillin ◽  
David L Amrani
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Point Mutation ◽  
Genomic Dna ◽  
Comparative Sequence Analysis ◽  
Chain Gene ◽  
Molecular Defect ◽  
Nucleotide Position ◽  
Normal Individuals ◽  
Polymerase Chain

SummaryParis I dysfibrinogenemia results in the production of a fibrinogen molecule containing a functionally abnormal γ-chain. We determined the basis of the molecular defect using polymerase chain reaction (PCR) to amplify the γ-chain region of the Paris I subject’s genomic DNA. Comparative sequence analysis of cloned PCR segments of normal and Paris I genomic DNA revealed only an A→G point mutation occurring at nucleotide position 6588 within intron 8 of the Paris I γ-chain gene. We examined six normal individuals and found only normal sequence in this region, indicating that this change is not likely to represent a normal polymorphism. This nucleotide change leads to a 45 bp fragment being inserted between exons 8 and 9 in the mature γparis I chain mRNA, and encodes a 15 amino acid insert after γ350 [M-C-G-E-A-L-P-M-L-K-D-P-C-Y]. Alternative splicing of this region from intron 8 into the mature Paris I γ-chain mRNA also results after translation into a substitution of S for G at position γ351. Biochemical studies of 14C-iodoacetamide incorporation into disulfide-reduced Paris I and normal fibrinogen corroborated the molecular biologic predictions that two additional cysteine residues exist within the γpariS I chain. We conclude that the insertion of this amino acid sequence leads to a conformationallyaltered, and dysfunctional γ-chain in Paris I fibrinogen.

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