|Byrd, James - Allen|
Submitted to: Poultry Science
Publication Type: Abstract only
Publication Acceptance Date: 7/24/2001
Publication Date: N/A
Citation: Interpretive Summary:
Technical Abstract: Previously, our laboratory has described a bursa of Fabricius-derived molecule that was named Bursal Anti-Steroidogenic Peptide (BASP) after its potent anti-steroidogenic activity. While the biological activity of BASP in several in vitro systems has been studied in our laboratory, until recently, molecular/structural characterization has remained elusive due lack of substantial amounts of highly purified biologically active material useful for conventional sequencing. Presently, endopeptidase digestion, fragment purification, and conventional N-terminus sequencing of each of the two predominant bands (24 and 30 kDa) from SDS PAGE of highly purified biologically-active BASP were performed and six low level sequences were determined. Each of these short fragment sequences showed homology with the known sequence of chicken histone H1. A single partial sequence homologous with the structure of chicken histone H1 was also obtained utilizing Q-TOF analysis. In addition, a unidirectional cDNA library constructed from bursa of Fabricius mRNA was screened with polyclonal antibody probes constructed against highly purified biologically active BASP. Six expression proteins were identified, and nucleotide sequencing of the lambda phage inserts revealed 4 unique partial nucleotide sequences from the 6 sequenced cDNA inserts. One of these nucleotide sequences (two overlapping cDNA insets) was 99% homologous with chicken histone H1. These observations may argue that BASP is either identical to, processed from, or shares homology with chicken histone H1. Purification of chicken histone H1 for bioassay has been initiated.