Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.
KTH, Superseded Departments, Biotechnology.ORCID iD: 0000-0003-0996-1644
Show others and affiliations
1995 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 92, no 1, 195-9 p.Article in journal (Refereed) Published
Abstract [en]

PR-39, a proline/arginine-rich peptide antibiotic, has been purified from pig intestine and later shown to originate in the bone marrow. Intending to isolate a clone for a human counterpart to PR-39, we synthesized a PCR probe derived from the PR-39 gene. However, when this probe was used to screen a human bone marrow cDNA library, eight clones were obtained with information for another putative human peptide antibiotic, designated FALL-39 after the first four residues. FALL-39 is a 39-residue peptide lacking cysteine and tryptophan. All human peptide antibiotics previously isolated (or predicted) belong to the defensin family and contain three disulfide bridges. The clone for prepro-FALL-39 encodes a cathelin-like precursor protein with 170 amino acid residues. We have postulated a dibasic processing site for the mature FALL-39 and chemically synthesized the putative peptide. In basal medium E, synthetic FALL-39 was highly active against Escherichia coli and Bacillus megaterium. Residues 13-34 in FALL-39 can be predicted to form a perfect amphiphatic helix, and CD spectra showed that medium E induced 30% helix formation in FALL-39. RNA blot analyses disclosed that the gene for FALL-39 is expressed mainly in human bone marrow and testis.

Place, publisher, year, edition, pages
1995. Vol. 92, no 1, 195-9 p.
National Category
Industrial Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-13359PubMedID: 7529412OAI: oai:DiVA.org:kth-13359DiVA: diva2:324519
Note
QC 20100615Available from: 2010-06-15 Created: 2010-06-15 Last updated: 2017-12-12Bibliographically approved
In thesis
1. Analysis of human gene transcripts: Identification and characterisation based on homology and differential expression
Open this publication in new window or tab >>Analysis of human gene transcripts: Identification and characterisation based on homology and differential expression
1998 (English)Doctoral thesis, comprehensive summary (Other scientific)
Place, publisher, year, edition, pages
Stockholm: KTH, 1998. 68 p.
National Category
Industrial Biotechnology
Identifiers
urn:nbn:se:kth:diva-2751 (URN)91-7170-347-0 (ISBN)
Public defence
1998-12-18, 00:00
Note
QC 20100615Available from: 2000-01-01 Created: 2000-01-01 Last updated: 2010-06-17Bibliographically approved

Open Access in DiVA

No full text

PubMed

Search in DiVA

By author/editor
Odeberg, Jacob
By organisation
Biotechnology
In the same journal
Proceedings of the National Academy of Sciences of the United States of America
Industrial Biotechnology

Search outside of DiVA

GoogleGoogle Scholar

pubmed
urn-nbn

Altmetric score

pubmed
urn-nbn
Total: 81 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf