Literature DB >> 3795272

Preliminary crystallographic studies on bovine lactoferrin.

G E Norris, B F Anderson, E N Baker, H M Baker, A L Gärtner, J Ward, S V Rumball.   

Abstract

The purification of bovine lactoferrin, its crystallization at low ionic strength, and preliminary X-ray crystallographic data are reported. The crystals, which grow from a two-phase system, are radiation-stable and suitable for a medium-resolution X-ray analysis. They are orthorhombic, space group P2(1)2(1)2(1), with cell dimensions a = 138.4 A, b = 87.1 A, c = 73.6 A, and one protein molecule in the asymmetric unit.

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Year:  1986        PMID: 3795272     DOI: 10.1016/0022-2836(86)90432-8

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus.

Authors:  Maria Grazia Ammendolia; Mariangela Agamennone; Agostina Pietrantoni; Fabio Lannutti; Rosa Anna Siciliano; Beatrice De Giulio; Carla Amici; Fabiana Superti
Journal:  Pathog Glob Health       Date:  2012-03       Impact factor: 2.894

2.  A Peptide Bond from the Inter-lobe Segment in the Bilobal Lactoferrin Acts as a Preferred Site for Cleavage for Serine Proteases to Generate the Perfect C-lobe: Structure of the Pepsin Hydrolyzed Lactoferrin C-lobe at 2.28 Å Resolution.

Authors:  Jiya Singh; Ankit Maurya; Prashant K Singh; V Viswanathan; Md Irshad Ahmad; Pradeep Sharma; Sujata Sharma; Tej P Singh
Journal:  Protein J       Date:  2021-11-03       Impact factor: 2.371

  2 in total

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