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Antimicrobial peptides in the stomach of Xenopus laevis

Autor: Kent Turner, Michael Zasloff, Howard Eck, Michael Brasseur, Karen Moore, Natale Tomassini, Charles L. Bevins

Publikováno v: Journal of Biological Chemistry. 266:19851-19857

Antimicrobial peptides are widely distributed in nature and appear to play a role in the host defense of plants and animals. In this study we report the existence of antimicrobial peptides in the stomach of the vertebrate Xenopus laevis, an animal pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ec869acaca31ebba4cff79213e9fb87e
https://doi.org/10.1016/s0021-9258(18)55069-9

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Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA

Autor: Howard Eck, Gill Diamond, Charles L. Bevins, Michael Zasloff, Michael Brasseur, W. L. Maloy

Publikováno v: Proceedings of the National Academy of Sciences. 88:3952-3956

Extracts of the bovine tracheal mucosa have an abundant peptide with potent antimicrobial activity. The 38-amino acid peptide, which we have named tracheal antimicrobial peptide (TAP), was isolated by a sequential use of size-exclusion, ion-exchange,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca1e9b8190451df5d148d6fc70cf1a25
https://doi.org/10.1073/pnas.88.9.3952

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Hb Shelby [beta 131(H9)Gln--Lys] in association with Hb S [beta 6(A3)Glu--Val]: characterization, stability, and effects on Hb S polymerization

Autor: Saul Surrey, Kazuhiko Adachi, Eric F. Rappaport, K Ohene-Frempong, Jungyop Kim, Howard Eck, H. Tamary

Publikováno v: Hemoglobin. 17(4)

When first tested for abnormal hemoglobins, a 2-year-old boy, appeared to have Hb F, Hb S and Hb A2. Confirmatory testing revealed a beta chain variant inherited from his father and beta S from his mother. Analysis of tryptic peptides in conjunction

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c80e7faaa960883b81e4024abf19a85
https://pubmed.ncbi.nlm.nih.gov/8226094

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Biologic and biochemic properties of recombinant platelet factor 4 demonstrate identity with the native protein

Autor: Saul Surrey, Mortimer Poncz, Kazuhiko Adachi, Howard Eck, Salahaldin Rifat, Kwang Sook Park

Publikováno v: Blood. 75(6)

Platelet factor 4 (PF4) is a 70 amino acid protein released from the alpha-granules of platelets after activation. The exact biologic function of this protein is unknown. We have constructed an expression vector for recombinant PF4 (rPF4) in the T7-b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5014e3d8301ccc8c94e6654ccb85ddee
https://pubmed.ncbi.nlm.nih.gov/2178704

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