Antigenic Determinants of Hen Egg White Lysozyme

Shinka, Sohei; Imanishi, Michiko; Miyagawa, N; Amano, Tsunehisa; Inouye, Masayori; Tsugita, Akira

doi:10.2183/pjab1945.43.505

Cited by 8 publications

(12 citation statements)

References 6 publications

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“…The resulting fragment consisted, therefore, of the sequences 64-83 and 91-107 or 91-108, connected by two disulfide bonds. The fragment contained some contamination of a larger peptide, similar t o the one reported by Shinka et al [15], which includes the section 57-63, and accounts for the presence of glutamic acid and for the higher contents of tryptophane (see Table 1). …”

Section: Discussionsupporting

confidence: 74%

“…I n this respect it exhibits very close similarity t o all the inhibitory peptides isolated and tested by Shinka et al [15]. This fact implies the presence of at least one, but possibly more, antigenic determinants.…”

Section: Discussionsupporting

confidence: 62%

“…Due to the flexible specificity of pepsin and to the differences in the conditions employed in the reaction, the peptides obtained were not identical. According to Shinka et al [15], even under a fixed set of conditions splitting by pepsin can occur in several places leading to the formation of similar but not identical peptides. However, in all the reported peptides the "loop" between the cysteine residues 64 and 80 was retained intact.…”

Section: Discussionmentioning

confidence: 99%

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A Selective Fractionation of Anti-Lysozyme Antibodies of Different Determinant Specificities

Arnon

1968

Eur J Biochem

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Antibodies to lysozyme were selectively fractionated by the use of an immunoadsorbent prepared with a peptic fragment of the enzyme, and a subsequent purification of the remaining antibodies in the serum. Both fractions of antibodies reacted immunologically with lysozyme as checked by antigen-combining and passive cutaneous anaphylaxis tests, but only the second fraction precipitated with it. Both fractions inhibited the catalytic activity of lysozymc, on a large substrate (Micrococcus Zysodeikticus) as well as on a substrate of small molecular weight (pentasaccharide), but to a lesser extent than the total antibody population. It is concluded that in the lysozyme-antilysozyme system the inhibition by the antibodies is due to steric hindrance alone. The greater inhibitory efficicncy of the unfractionated antilysozyme antibodies, seems due to simultaneous combination of the enzyme with several antibody molecules of diEerent specificities.

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Section: Discussionsupporting

confidence: 74%

Section: Discussionsupporting

confidence: 62%

Section: Discussionmentioning

confidence: 99%

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A Selective Fractionation of Anti-Lysozyme Antibodies of Different Determinant Specificities

Arnon

1968

Eur J Biochem

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“…The results observed between hen egg-white lysozyme and bovine a-lactoalbumine indicated a cross reaction with regard to the delayed-type hypersensitivity level but no cross reaction with each other on the circulating antibody level (Maron et al, 1972). It was already shown by Shinka et al (1967) and Fujio et al (1968) that their fractions 7 and 17 isolated from the pepsin digest of hen egg-white lysozyme had an antigenic activity against rabbit antilysozyme serum. We also separated 11 fractions from pepsin-digested lysozyme by the same method as Shinka et al (1967).…”

Section: Introductionmentioning

confidence: 65%

“…It was already shown by Shinka et al (1967) and Fujio et al (1968) that their fractions 7 and 17 isolated from the pepsin digest of hen egg-white lysozyme had an antigenic activity against rabbit antilysozyme serum. We also separated 11 fractions from pepsin-digested lysozyme by the same method as Shinka et al (1967). Our fractions PP-3 and PP-9 were correspond to their Fr.…”

Section: Introductionmentioning

confidence: 85%