Výsledky vyhledávání - "PADMAJA JUVVADI"

Synthesis and antibacterial action of cecropin and proline-arginine-rich peptides from pig intestine

Autor: Satyanarayana Vunnam, Padmaja Juvvadi, R. B. Merrifield

Publikováno v: The Journal of Peptide Research. 49:59-66

Two antimicrobial peptides, cecropin P1 (CP1), with a C-terminal carboxyl group, and PR-39, with an amidated, C-terminus, are found in the small intestine of the pig. Each is active against both Gram-positive and Gram-negative bacteria. We have synth

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb18e7176dc1c132371e43f0fa6fceff
https://doi.org/10.1111/j.1399-3011.1997.tb01121.x

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Ouabain and substrate affinities of human Na+-K+-ATPase α1β1, α2β1, and α3β1when expressed separately in yeast cells

Autor: Robert H. G. Schwinger, Michelle L. Croyle, Robert A. Farley, Jerry B. Lingrel, Lusine Tumyan, Curtis B. Thompson, Padmaja Juvvadi, Jochen Müller-Ehmsen, Alicia A. McDonough

Publikováno v: American Journal of Physiology-Cell Physiology. 281:C1355-C1364

Human Na+-K+-ATPase α1β1, α2β1, and α3β1heterodimers were expressed individually in yeast, and ouabain binding and ATP hydrolysis were measured in membrane fractions. The ouabain equilibrium dissociation constant was 13–17 nM for α1β1and α

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f0bec03351df1d1d4ea7f6334d49fc92
https://doi.org/10.1152/ajpcell.2001.281.4.c1355

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Orientation of Cecropin A Helices in Phospholipid Bilayers Determined by Solid-State NMR Spectroscopy

Autor: Stanley J. Opella, R. B. Merrifield, Francesca M. Marassi, Padmaja Juvvadi

Publikováno v: Biophysical Journal. 77:3152-3155

The orientation of the insect antibiotic peptide cecropin A (CecA) in the phospholipid bilayer membrane was determined using (15)N solid-state NMR spectroscopy. Two peptide samples, each specifically labeled with (15)N at Val(11) or Ala(27), were syn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86de44191c4ebc8821a63ae7f9b3e0f6
https://doi.org/10.1016/s0006-3495(99)77145-6

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Structure-activity studies of normal and retro pig cecropin-melittin hybrids

Autor: Padmaja Juvvadi, Barney Yoo, Satyanarayana Vunnam, R. B. Merrifield

Publikováno v: The Journal of Peptide Research. 53:244-251

Chimeric analogs of cecropin P1 and melittin with normal and retro sequences were synthesized to explore the effect of sequence, amide bond direction (helical dipole), charge, amphipathicity and hydrophobicity on their antibacterial activity and chan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6f73d2eb809107ec001fda7a3bdc1def
https://doi.org/10.1034/j.1399-3011.1999.00020.x

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7Li and23Na NMR studies of transmembrane cation transport mediated by ionophore lasalocid A

Autor: Padmaja Juvvadi, Easwaran Kalapaty

Publikováno v: Journal of Peptide Science. 4:15-20

Ion transport across phospholipid vesicles was studied by 7Li and 23Na-NMR using an aqueous anionic paramagnetic shift reagent, dysprosium nitrilotriacetate [Dy(NTA)2]3?, mediated by ionophores, lasalocid A and A23187. The intra- and extracellular 7L

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d4a81605ca63cd508fa3be076861553
https://doi.org/10.1002/(sici)1099-1387(199802)4:1<15::aid-psc96>3.0.co

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