Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.30.2 (endonuclease)
 18,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Preparations of human leukocyte interferon obtained by multi-stage purification procedure exhibited ribonuclease activity with the optimum at pH 7.0--7.5. The enzyme possessed the endonuclease action mechanism. Most substances studied for their effect on the RNA-ase activity in human interferon preparations showed many of them to act on the enzyme in the same way as on other ribonucleases. However, dithioerythritie, a reducing agent for disulfide bounds, activated the ribonuclease in the interferon preparation, as distinct from the pancreatic ribonuclease, which was inhibited by this preparation. Patterns of protein and RNA-ase distribution were obtained by electrophoresis in polyacrylamide gel.
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PMID:[Ribonuclease activity in preparations of human leukocyte interferon]. 0 77

Two deoxyoctadecyloligonucleotides complementary to the sequence spanning a single base substitution between human leukocyte interferon (HuIFN) alpha A and alpha 2 genes were efficiently used as probes to distinguish between HuIFN-alpha A and -alpha 2 genes. At 37 degrees C or 42 degrees C under aqueous conditions (0.9 M NaCl), hybridization between both probes and the alpha A and alpha 2 genes without any mismatch was strong, whereas the hybridization with one base mismatch (alpha A probe-alpha 2 gene and alpha 2 probe-alpha A gene) was very weak or negligible. Because the single base substitution of G in the alpha 2 gene for A in the alpha A gene provides an extra HinfI site in the alpha 2 gene at the center of the sequence hybridizing to the alpha 2 probe, digestion with HinfI restriction endonuclease caused complete loss of the hybridization between the alpha 2 probe and the alpha 2 gene. PvuII digestion provides 298-bp fragments hybridizing to the probes only from the alpha A and alpha 2 genes among the known HuIFN-alpha genes. Thus, with the use of these oligonucleotide probes in combination with PvuII and PvuII-HinfI restriction endonuclease digestion, the existence of the sequences corresponding to both IFN-alpha A and IFN-alpha 2 genes in human genomic DNAs was demonstrated. The results also surprisingly indicate that these genes, formerly considered alleles because of their essential identity (1 base pair difference in the coding sequence), are not likely to be alleles, but represent closely related distinct genes.
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PMID:Detection of human leukocyte interferon-alpha A and -alpha 2 genes in genomic DNAs by the use of deoxyoctadecyloligonucleotide probes. 283 13

By using blot hybridization with a v-fms probe, a polymorphism for EcoRI, HindIII, and BamHI restriction endonuclease sites associated with the human c-fms locus was observed in a random adult population. This restriction fragment length polymorphism can be explained on the basis of the existence of two alleles, a and b, and is due to a short (congruent to 500 base pairs) deletion characteristic of allele a. The distribution in the analyzed population (48 unrelated individuals) is 23% heterozygotes ab, 75% homozygotes bb, and 2% homozygotes aa. Though the inheritance of this polymorphism follows a Mendelian pattern, the children from couples ab X bb are of the following genotype: 74% ab and 26% bb. These deviations from the expected frequencies of 50% suggest a selective pressure in favor of heterozygotes.
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PMID:Restriction fragment length polymorphism of the human c-fms gene. 298 42

Four hybrid human leukocyte interferon (LeIF or IFN-alpha) genes have been constructed by in vitro recombination of LeIF-A (IFN-alpha 2) and LeIF-D (IFN-alpha 1) genes at common restriction endonuclease sites located within their coding regions. These hybrid genes have been expressed in E. coli under trp promoter control. The interferons produced [LeIF-AD (BglII), -AD (PvuII), -DA (BglII), -DA (PvuII)] have antiviral properties distinct from the parental molecules LeIF-A and -D, varying considerably in their abilities to inhibit plaque formation by different viruses in a range of mammalian cells. All six of the cloned LeIFs exhibit the heat stability, pH 2 stability and antigenic specificity of natural leukocyte interferons.
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PMID:Antiviral activities of hybrids of two major human leukocyte interferons. 617 79

Eleven chimeric plasmids have been constructed which direct the synthesis of mature human fibroblast (IFN-beta 1) or leukocyte interferon (IFN-alpha A) proteins under the control of the E. coli trp promoter. The plasmids differ with respect to the nucleotide spacing between the Shine-Dalgarno sequence of the trp leader and the ATG translation start signal of the interferon genes. By utilizing a unique Xba I endonuclease site located within the spacer region of the expression plasmids, the spacings were altered from 2-10 nucleotides or 7-15 nucleotides for the fibroblast and leukocyte interferon expression plasmids, respectively. The optimal spacing for expression, as determined by interferon assay, is 9 nucleotides for both types of transcripts, despite differences in nucleotide sequence within the spacer region and downstream from the AUG initiator. Yields of IFN-alpha A varied about six-fold, while among the different IFN-beta 1 expression plasmids a range of more than 100-fold in interferon production was observed. The difference in the range of variation between the IFN-alpha A and IFN-beta 1 plasmids is attributed partly to changes in messenger RNA secondary structure within the ribosome binding sites which affect message half-life.
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PMID:Increased synthesis in E. coli of fibroblast and leukocyte interferons through alterations in ribosome binding sites. 618 21

Four hybrid human leukocyte interferon (IFN-alpha) genes have been constructed and expressed in Escherichia coli using molecular cloning methods. Plasmids containing genes encoding human interferons, IFN-alpha A, IFN-alpha D, IFN-alpha I and several hybrids of the different IFN-alpha genes (formed by in vitro recombination at common restriction endonuclease sites located within the DNA sequence encoding mature polypeptides) joined identically to an E. coli trp promoter gave rise to bacterial-produced interferons with distinctly different antiviral activities. The expression plasmid which directs the synthesis of IFN-alpha I was constructed using a gene isolated from a human genomic library in a manner similar to the previous expression of IFN-alpha A and IFN-alpha D cDNA clones. The use of a cell-free transcription-translation system has allowed the calculation of the specific activities of IFN-alpha made from isolated DNA fragments containing these hybrid IFN-alpha genes. These bacterially-derived interferons vary considerably in their ability to inhibit vesicular stomatitis virus (VSV) in different mammalian cells. The results show that the cloned hybrid interferons have unique antiviral activities when compared with the parent interferons, and they demonstrate that more active IFN-alpha s can be made using recombinant DNA techniques.
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PMID:Carboxyterminal region of hybrid leukocyte interferons affects antiviral specificity. 630 84

A restriction fragment length polymorphism (RFLP) for the c-fms gene was identified in the human oral squamous cell carcinoma cell lines, Ca9-22, HSC-2 and -3. The RFLP was detected after EcoR I, BamH I and Hind III endonuclease digestion, indicating the presence of two alleles, a and b. The allele a deleted 426bp length of allele b. We determined the sequence of this deletion, that localized in intron 11 with an EcoR I site. The phenotype of Ca9-22 was aa, and the others were bb. Both phenotypes were equally expressed and the transcripts were phosphorylated in these cell lines. The distribution in the analyzed population (66 patients and normal individuals) was 3.1% homozygotic aa, 13.5% heterozygotic ab and 83.4% homozygotic bb.
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PMID:Restriction fragment length polymorphism of the c-fms gene in the human oral squamous cell carcinomas. 791 38