The structure of the acidic polypeptide chains from alpha-crystallin. Amino acid composition, peptide mapping, and N-terminus.

THE STRUCTURE OF THE ACIDIC POLYPEPTIDE CHAINS FROM a-CRYSTALLIN. AMINO ACID COMPOSITION, PEPTIDE MAPPING, AND N-TERMINUS

Location of a polypeptide sequence within the alpha-subunit of the acetylcholine receptor containing the cholinergic binding site.

Proteolytic fragments of the alpha-subunit of the acetylcholine receptor of Torpedo electric organ were generated by digestion with Staphylococcus aureus V8 protease, and their ability to bind alpha-bungarotoxin was assessed following resolution on polyacrylamide gels and transfer to nitrocellulose. The position of the smallest fragment (Mr = 17,000) with toxin-binding activity was located with...

Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity

Recently, antimicrobial peptides have been introduced as potent antibiotics with a wide rangeof antimicrobial activities. They have also exhibited other biological activities, including antiinflammatory,growth stimulating, and anti-cancer activities. In this study, an analog of MagaininII was designed and produced as a recombinant fusion protein. The designed sequence containe...

Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity

Recently, antimicrobial peptides have been introduced as potent antibiotics with a wide rangeof antimicrobial activities. They have also exhibited other biological activities, including antiinflammatory,growth stimulating, and anti-cancer activities. In this study, an analog of MagaininII was designed and produced as a recombinant fusion protein. The designed sequence containe...

Human alpha-crystallin. I. The isolation and characterization of newly synthesized alpha-crystallin.

Studies of the incorporation of 14C amino acids into human lens proteins demonstrate that an alpha-crystallin fraction takes up more than six times as much radioactivity as any other lens protein. Based on analyses with a calibrated Bio-Gel A-1.5 m column, a molecular weight of 4.9 x 10(5) +/- 5 per cent was obtained for this protein while sedimentation equilibrium analyses indicated a weight a...