Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.26.9 (ribonuclease)
 6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

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