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Related Experiment Videos

Domain structure and sequence distribution in dentin phosphophoryn.

B Sabsay1, W G Stetler-Stevenson, J H Lechner

  • 1Northwestern University, Division of Oral Biology, Chicago, IL 60611.

The Biochemical Journal
|June 15, 1991
PubMed
Summary
This summary is machine-generated.

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Phosphophoryn (PP), a dentin protein rich in aspartic acid and phosphoserine, was analyzed using acid hydrolysis and trypsin digestion. This revealed distinct acidic domains, aiding in understanding its structure and function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biomineralization

Background:

  • Phosphophoryn (PP) is a unique protein found in the mineralized matrix of dentin.
  • PP has an unusual amino acid composition, with >85% aspartic acid and phosphoserine.
  • Its composition complicates direct peptide sequencing, hindering functional studies and cDNA library screening.

Purpose of the Study:

  • To determine sequence distribution information for phosphophoryn (PP).
  • To understand the function of PP and prepare probes for cDNA library screening.
  • To elucidate the domain structure of PP.

Main Methods:

  • Partial mild acid hydrolysis of bovine and rat incisor PPs to cleave aspartic acid residues.
  • Limited digestion with trypsin to generate peptides.

Related Experiment Videos

  • Purification of peptides using h.p.l.c. and subsequent sequencing.

    • Main Results:

    • Approximately 90% of PPs were resistant to trypsin, forming a fragment depleted of non-aspartic acid and non-phosphoserine residues.
    • Isolated peptides were acidic.
    • Non-aspartic acid and non-phosphoserine residues were located in regions flanking the trypsin-resistant core.

    Conclusions:

    • The data confirm the presence of prominent sequence features such as [Asp]n, [(P)Ser]m, and [Asp-(P)Ser-Asp]k regions.
    • A domain structure model for phosphophoryn is proposed based on these findings.
    • This structural information is crucial for understanding PP's role in dentin.