Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Guadalupe A. Limjuco"'
Autor:
Kevin T. Chapman, Jeffrey R. Weidner, Ellen K. Bayne, Jayne Chin, S Scott, Irwin I. Singer, Matthew J. Kostura, Douglas K. Miller, Guadalupe A. Limjuco
Publikováno v:
The Journal of Experimental Medicine
Interleukin-1 beta (IL-1 beta)-converting enzyme (ICE) is a novel cysteine protease that cleaves the 31-kD inactive cytoplasmic IL-1 beta precursor into active extracellular 17-kD IL-1 beta. The ICE gene product is a 45-kD proenzyme that requires pro
Autor:
John A. Schmidt, Matthew J. Kostura, Anna M. Rolando, Richard A. Mumford, Ting-Ting Yamin, Guadalupe A. Limjuco, Keith O. Elliston, Jeffrey R. Weidner, J. Paul Salley, Jayne Chin, Susan M. Molineaux, S.M. Raju, John G. Aunins, Gloria J.-F. Ding, Douglas K. Miller, John E. Shively, Oksana C. Palyha, Julia M. Ayala, Nancy A. Thornberry, Michael J. Tocci, Malcolm MacCross, Francesca J. Casano, Herbert G. Bull, Andrew D. Howard, Linda A. Egger, Kevin T. Chapman, Jimmy R. Calaycay, Erin P. Gaffney, Terry D. Lee
Publikováno v:
Nature. 356:768-774
Interleukin-1 beta (IL-1 beta)-converting enzyme cleaves the IL-1 beta precursor to mature IL-1 beta, an important mediator of inflammation. The identification of the enzyme as a unique cysteine protease and the design of potent peptide aldehyde inhi
Autor:
E P Peterson, T T Yamin, Francesca J. Casano, Jimmy R. Calaycay, Jayne Chin, Susan M. Molineaux, Patrick R. Griffin, Gloria J.-F. Ding, Guadalupe A. Limjuco, Anna M. Rolando
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 90(5)
Murine interleukin 1 beta (IL-1 beta) convertase (mICE) was identified in cytosolic extracts of peritoneal exudate cells (PECs) and macrophage cell lines. mICE cleaves both the human and mouse IL-1 beta precursors (pIL-1 beta) at sites 1 and 2 but fa
Publikováno v:
The Journal of Immunology. 115:1731-1743
Four glycoproteins (GP1, 2, 3, and 4) rich in carbohydrate were isolated from guinea pig testes. GP1, 2, and 4 (one or more) were localized in the sperm acrosome by the indirect immunofluorescence technique. Purification consisted of delipidation wit
Autor:
Robert Z. Maigetter, Guadalupe A. Limjuco, Johanna Y. Zeltner, Dennis J. Carlo, Yashwant D. Karkhanis, J. J. King
Publikováno v:
Journal of General Microbiology. 104:187-191
SUMMARY: A lipopolysaccharide was isolated from Neisseria meningitidis group B by phenol/water extraction and purified by differential ultracentrifugation. This preparation exhibited endotoxic properties as shown by the limulus-lysate assay. Mild aci
Publikováno v:
The Journal of Experimental Medicine
The pI-6.8 species of normal human interleukin 1 (IL-1) has been isolated by ion-exchange and reverse-phase high-performance liquid chromatography. The isolated material had a molecular weight of 18,000, and had a specific bioactivity of 1.7 X 10(7)
Autor:
Jayne Chin, Guadalupe A. Limjuco, Patricia M. Cameron, John A. Schmidt, Leslie E. Silberstein
Publikováno v:
The Journal of Experimental Medicine
Two anionic species of human IL-1 have been purified to homogeneity. These molecules were characterized as having pI of 5.4 and 5.2 and molecular weights identical to IL-1/6.8 (17,500). The specific activities of IL-1/5.4 and IL-1/5.2, as measured in
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 427:251-261
The AP1 protein, a unique aspermatogenic protein localized in the sperm acrosome, exists as a single polypeptide chain of 136 amino acids, as shown by a single band on gel electrophoresis in sodium dodecyl sulfate and the recovery of the expected 21
Autor:
Guadalupe A. Limjuco, Jayne Chin, Patricia M. Cameron, Nicole A. Chartrain, John A. Schmidt, Matthew J. Kostura, Andrew G. Hillman, Michael J. Tocci
Publikováno v:
Proceedings of the National Academy of Sciences. 86:5227-5231
Interleukin 1 (IL-1) is a lymphokine secreted by monocytes in response to a variety of inflammatory stimuli. IL-1 beta, the predominant form of IL-1 produced by human monocytes, is synthesized as an inactive precursor of 31 kDa and is cleaved at Asp1
Autor:
Stefan Galuska, Joshua S. Boger, Jayne Chin, John A. Schmidt, Guadalupe A. Limjuco, Patricia M. Cameron
Publikováno v:
Proceedings of the National Academy of Sciences. 83:3972-3976
The development of highly specific antisera to human interleukin 1 (IL-1) has been an elusive goal hampered mainly by the availability of only limited amounts of pure immunogen. To surmount this difficulty, three peptides of the major charged species