Mass spectrometric analysis of enzymatic digestion of denatured collagen for identification of collagen type.
Collagen type II and I from bovine were thermally denatured and digested with trypsin. The digest mixture was analyzed with liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS). Peptides in the digest mixture were identified by mass spectrometry/mass spectrometry (MS/MS) sequencing. The results indicated that the digest mixtures of collagen type II and I contained lots of specific peptides and common peptides. Specific peptides could be used as index for identifying collagen type. Articular cartilage from bovine was pretreated and analyzed with the same method to determine the collagen types. The result indicated that the method developed was effective for identification of collagen types. The research provided a possible approach for collagen identification in particular tissues.
Zhang
Guifeng
G
State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100080, PR China.
Sun
Aimei
A
Li
Weijun
W
Liu
Tao
T
Su
Zhiguo
Z
D000818:Animals; D002358:Cartilage, Articular / Q000737:chemistry; D002417:Cattle; D003094:Collagen / Q000032:analysis* / Q000737:chemistry*; D024042:Collagen Type I / Q000032:analysis; D024043:Collagen Type II / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis / Q000302:isolation & purification; D011489:Protein Denaturation; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014357:Trypsin / Q000378:metabolism
D024042:Collagen Type I; D024043:Collagen Type II; D010446:Peptide Fragments; D003094:Collagen; D014357:Trypsin