Structural analysis of the extension peptides on matrix forms of type V collagen in fetal calf bone and skin

Christopher Niyibizi, David R. Eyre

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31 Citations (Scopus)

Abstract

The structure of the extension peptides retained on the tissue form of type V collagen molecules was determined. Type V collagen α chains containing extension peptides were extracted from fetal calf skin and bone by 4 M guanidine-HCl and 0.5 M acetic acid, respectively. Collagens present in both extracts were fractionated by sodium chloride precipitation. The collagen α(V) chains were then resolved by reverse-phase high performance liquid chromatography. The N-terminal extension peptides were characterized by direct sequence analysis after deblocking with pyroglutamate amino-peptidase and analysis of the products of digestion by bacterial collagenase, chymotrypsin, V8 protease and endoproteinase Lys-C. The results showed that the retained extension peptides on type V collagen molecules in the extracellular matrix of skin and bone were amino-properties and that the α2(V) chain retains an intact amino-propeptide while the α1(V) chain appears to be partially processed. The extended α1(V) chain isolated from fetal calf bone gave an identical amino-terminal sequence to that of the α1(V) chain isolated from fetal calf skin, suggesting that a specific enzyme may be involved in processing the α1(V) amino-propeptide.

Original languageEnglish (US)
Pages (from-to)304-309
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1203
Issue number2
DOIs
StatePublished - Dec 8 1993

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Collagen Type V
Structural analysis
Skin
Bone
Collagen
Bone and Bones
Peptides
Pyrrolidonecarboxylic Acid
Guanidine
Chymotrypsin
Collagenases
Reverse-Phase Chromatography
Sodium Chloride
Acetic Acid
Molecules
Extracellular Matrix
Sequence Analysis
Digestion
High performance liquid chromatography
Peptide Hydrolases

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

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abstract = "The structure of the extension peptides retained on the tissue form of type V collagen molecules was determined. Type V collagen α chains containing extension peptides were extracted from fetal calf skin and bone by 4 M guanidine-HCl and 0.5 M acetic acid, respectively. Collagens present in both extracts were fractionated by sodium chloride precipitation. The collagen α(V) chains were then resolved by reverse-phase high performance liquid chromatography. The N-terminal extension peptides were characterized by direct sequence analysis after deblocking with pyroglutamate amino-peptidase and analysis of the products of digestion by bacterial collagenase, chymotrypsin, V8 protease and endoproteinase Lys-C. The results showed that the retained extension peptides on type V collagen molecules in the extracellular matrix of skin and bone were amino-properties and that the α2(V) chain retains an intact amino-propeptide while the α1(V) chain appears to be partially processed. The extended α1(V) chain isolated from fetal calf bone gave an identical amino-terminal sequence to that of the α1(V) chain isolated from fetal calf skin, suggesting that a specific enzyme may be involved in processing the α1(V) amino-propeptide.",
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AU - Eyre, David R.

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N2 - The structure of the extension peptides retained on the tissue form of type V collagen molecules was determined. Type V collagen α chains containing extension peptides were extracted from fetal calf skin and bone by 4 M guanidine-HCl and 0.5 M acetic acid, respectively. Collagens present in both extracts were fractionated by sodium chloride precipitation. The collagen α(V) chains were then resolved by reverse-phase high performance liquid chromatography. The N-terminal extension peptides were characterized by direct sequence analysis after deblocking with pyroglutamate amino-peptidase and analysis of the products of digestion by bacterial collagenase, chymotrypsin, V8 protease and endoproteinase Lys-C. The results showed that the retained extension peptides on type V collagen molecules in the extracellular matrix of skin and bone were amino-properties and that the α2(V) chain retains an intact amino-propeptide while the α1(V) chain appears to be partially processed. The extended α1(V) chain isolated from fetal calf bone gave an identical amino-terminal sequence to that of the α1(V) chain isolated from fetal calf skin, suggesting that a specific enzyme may be involved in processing the α1(V) amino-propeptide.

AB - The structure of the extension peptides retained on the tissue form of type V collagen molecules was determined. Type V collagen α chains containing extension peptides were extracted from fetal calf skin and bone by 4 M guanidine-HCl and 0.5 M acetic acid, respectively. Collagens present in both extracts were fractionated by sodium chloride precipitation. The collagen α(V) chains were then resolved by reverse-phase high performance liquid chromatography. The N-terminal extension peptides were characterized by direct sequence analysis after deblocking with pyroglutamate amino-peptidase and analysis of the products of digestion by bacterial collagenase, chymotrypsin, V8 protease and endoproteinase Lys-C. The results showed that the retained extension peptides on type V collagen molecules in the extracellular matrix of skin and bone were amino-properties and that the α2(V) chain retains an intact amino-propeptide while the α1(V) chain appears to be partially processed. The extended α1(V) chain isolated from fetal calf bone gave an identical amino-terminal sequence to that of the α1(V) chain isolated from fetal calf skin, suggesting that a specific enzyme may be involved in processing the α1(V) amino-propeptide.

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