Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.27.1 (
RNase
)
16,360
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The purpose of this study was to investigate the in situ hybridization technique of paraffin-embedded skeletal tissues by non-radioactive labelling oligonucleotide, Five six-week-old male SD rats were selected and the proximal epiphyseal growth plates of bilateral tibiae were removed to be decalcified in 0.5 mol/L EDTA. The tissues were embedded by paraffin and the sections were treated and hybridized with
RNase
-free reagents. Control groups were set to testified the sensitivity and the specificity of the experiment. The results showed that this method preserved the integrate structures and effectively detected the mRNA of the tissues. These indicated that it was an efficient and practical approach to the biomolecular research of skeletal tissue.
Hua
Xi Kou Qiang Yi Xue Za Zhi 1998 Feb
PMID:[In situ hybridization with digoxigenin-labelling oligonucleotide: an practical approach to skeletal tissues]. 1207 82
Liquid chromatography-electrospray mass spectrometry was utilized to analyze peptide mapping of a glycoprotein
ribonuclease
B to obtain its primary structure. The glycosylated site was determined by comparison of peptide mapping before and after glycanase treatment.Tandem MS(MS/MS)was performed to analyze the structure of N-linked glycan and deglycosylated peptide. The nature of glycan was determined to be of highmannose type by mass spectrometry after the treatment with alpha-mannosidase. In addition the relative abundance of heterogeneous glycopeptides was quantified. This method is rapid and sensitive for the characterization of glycoproteins with N-linked glycan.
Sheng Wu
Hua
Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 1999
PMID:Analysis of Peptide Mapping Glycosylated Site and Glycan Structure in Ribonuclease B by Liquid Chromatography-Electrospray Mass Spectrometry. 1211 Sep 38
Protein disulfide-isomerase has been isolated from human liver. The preparative procedure involved heat treatment, (NH(4))(2)SO(4) precipitation, CM-Sephadex C50 and DEAE-fast flow chromatography. The enzyme was homogenous and had a molecular mass of 60 kD or 120 kD as determined by sodium dodecy1 sulphate electro-phoresis and gel filtration respectively, indicating that the enzyme was a 120 kD dimmer with a subunit with molecular mass of 60 kD. The enzyme activity was as high as 830 U/g.protein as measured by the reactivation of "scrambled"
ribonuclease
. The antiserum of high titer was prepared by immunizing New Zealand rabbit with a mixture of the protein disulfide-isomerase and adjuvant.
Sheng Wu
Hua
Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 1996
PMID:Purification of Protein Disulfide-isomerase from Human Liver and Preparation of Its Antiserum. 1223 36
Murine erythroleukemia (MEL) cell line was used as a model to evaluate the potential value of retroviral construct containing human beta-globin express io n cassette in gene therapy of beta-thalassemia and to explore possible mechanisms underlying low expression of retrovirally cloned human beta-globin gene. A recombinant retroviral vector was constructed, which harbored 2.0 kb beta-globin gene w it h a 374 bp deletion in intervening sequence II coupled with a mini locus control region (miniLCR) composed of DNaseI hypersensitive sites (HS) 2 and 3 from human beta-LCR. The recombinant retroviruses were generated from an established psi-2 producer cell line, and by transient transfection of amphotropic packaging cell l ine psi-A, respectively. The integrity of provirus in transduced MEL cells was determined using Southern blot, and the expression of transferred human beta-globin gene was detected using
RNase
protection assay. The structure of provirus was further analyzed by sequence analysis of PCR products from genomic DNA of MEL individual clone as template. The results demonstrated that the average expression of human beta-globin gene was (52.4-/+11.2)% (n=12) and (73.8-/+14.3)% (n=12, without copy-number determination), compared with that of endogenous murine alpha-globin ge ne, in MEL cells transduced with the recombinant retrovirus from transient transfection of psi-A and MEL cells transfected with the construct, respectively. In M EL cells transduced with virus from psi-2 producer cell line, however, the average expression was less than 3%. A point mutation was detected in HS2 of provirus i n MEL cell clone with low expression of human beta-globin gene. The possible mechanisms involved in low expression, including position effect, DNA methylation a nd RNA interference are discussed in addition to the point mutation.
Sheng Wu
Hua
Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 2002 Nov
PMID:[The possible mechanisms underlying low expression of human beta-globin gene cloned in a retroviral vector]. 1241 21
Angiogenin (ANG), the fifth member of the vertebrate-specific
ribonuclease
(
RNase
) A superfamily, is a secreted angiogenic
ribonuclease
strongly up-regulated in human prostate cancers. ANG is translocated to the nucleus in both prostate cancer epithelial cells and endothelial cells to exert its role in prostate cancer progression by mediating tumor angiogenesis, cancer cell survival and proliferation through rRNA biogenesis. ANG-stimulated rRNA is required not only for prostate intraepithelial neoplasia (PIN) formation, but also for androgen-independent growth of prostate cancer cells. Targeting ANG by various antagonists that inhibit its nuclear translocation, function and/or activity has proven to inhibit prostate cancer growth in animal models. Furthermore, the role of ANG in androgen independence has been firmly established, suggesting a strong rationale for therapeutically targeting ANG in the treatment of castration resistant prostate cancer.
Zhongguo Sheng Wu
Hua
Xue Yu Fen Zi Sheng Wu Xue Bao 2015 Dec 20
PMID:Mechanism and Function of Angiogenin in Prostate Cancer. 2717 49
Angiogenin (ANG), a secreted
ribonuclease
, has been characterized recently as an anti-apoptosis factor involved in a variety of cellular anti-apoptosis process. ANG regulates intrinsic pathways-related major molecules such as anti-apoptotic protein Bcl-2, as well as extrinsic signaling pathways. Moreover, ANG regulates p53-regulated apoptosis, a process considered to be important in regulating both the extrinsic and the intrinsic pathways.
Zhongguo Sheng Wu
Hua
Xue Yu Fen Zi Sheng Wu Xue Bao 2015 Dec
PMID:Mechanism and Function of Angiogenin in Apoptosis Regulation. 2764 41