Lin L and Liu TY (1993), Isolation and characterization of C-reactive pr...

XB-ART-22735

J Biol Chem 1993 Mar 25;2689:6809-15.

Show Gene links Show Anatomy links

Isolation and characterization of C-reactive protein (CRP) cDNA and genomic DNA from Xenopus laevis. A species representing an intermediate stage in CRP evolution.

Lin L, Liu TY.

???displayArticle.abstract???

???displayArticle.pubmedLink??? 8454653
???displayArticle.link??? J Biol Chem

Species referenced: Xenopus laevis
Genes referenced: crp crp.2 crp.3 crp.4 crpl

???attribute.lit??? ???displayArticles.show???

	FIG. 1. SDS-PAGE of Xenopus CRP purified by the PC column. The gel is 8-25% acrylamide using the Laemmli system. Lane I, reduced Xenopus CRP; lane 2, nonreduced Xenopus CRP. A, Coomassie Blue staining. B, Western blot analysis using antipeptide antibody.
	FIG. 2. SDS-PAGE analysis of Xenopus CRP in serum. The gel is 16% acrylamide using the Laemmli system. Lane 1, under reducing condition; lane 2, under nonreducing condition. A, Coomassie Blue staining. B, Western blot analysis using antipeptide antibody.
	FIG. 3. Cloning of the cDNA and the Xenopus CRP. the Restriction map subclones of . Xenopus CRP cDNA and genomic fragments B, BamHI; E, EcoRI; H, HindIII; P, PstI. Exon 1 is the black box; Exon 2 and 3 are hatched boxes.
	FIG. 4. Sequence of Xenopus CRP. Nucleotide and deduced amino acid sequence of Xenopus CRP gene. For nucleotide sequence, the translational initiation site isd esignated as nucleotide 1. cDNA sequence identical to genomic sequence is expressed as dash lines. Polyadenylation signal is underlined. Intron sequences are in brackets. For amino acid, negative numbers correspond to the signal peptide, while positive numbers represent residues of the mature protein. Amino acid residues in parentheses are derived from cDNA sequence. Regions to which oligonucleotides were synthesized as primers for the polymerase chain reaction are underlined. Also underlined are the amino-terminal sequences determined by Edman degradation; upper line, from intact protein sequencing; lower line, regions to which oligonucleotides were synthesized.
	FIG. 5. Western blot analysis of Xenopus CRP gene expression. Sera from control and turpentine-treated frogs were subjected to Western blot analysis. Frogs 1-3, untreated; and frogs 4-6, turpentine- injected. Three pg of serum protein was electrophoresed on a 16% polyacrylamide gel, transferred onto Immobilon membrane and CRP was detected using CRP-specific anti-peptide antibody as described under Experimental Procedures.
	FIG. 6. Northern blot analysis of RNAs from various developmental stages. Total RNAs were isolated from Xenopus eggs (0) or from embryos at stages 7,10,16, 23,31, and 40. Twenty pg of each was electrophoresed onto a 1.2% agarose/formaldehyde gel. The RNA was transferred onto Gene Screen Plus membrane and hybridized with 32P-radiolabeled XCRP-cl fragment. A, autoradiogram; B, ethidium bromide staining.
	FIG. 7. Amino acid sequence comparison of mature human and Xenopus CRPs. Human CRP and Xenopus CRP sequences (derived boxed and numbered. from genomic sequence) were aligned using the Genetics Computer Group sequence analysis software package. The conserved regions were