The microfibrillar proteins of human hair: separation by high-performance liquid chromatography and isolation of some proteins enriched in glycine and tyrosine.
The microfibrillar proteins of human hair have been studied by reversed-phase high-performance liquid chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A chromatographic procedure which isolates the microfibrillar proteins from other hair-matrix proteins and separates them into collectable fractions has been introduced. These fibrous proteins fall into two major subgroups which are resolved into six components. The same procedure has also resulted in the identification and simultaneous separation of a group of proteins rich in glycine and tyrosine never before detected in human hair. Comparative electrophoretic studies of the crude microfibrillar proteins reveal five bands with apparent molecular weights of 47,000, 50,000, 53,000, 57,000, and 62,000. The relationship between the electrophoretic bands and the chromatographic fractions is now under investigation.
Redken Laboratories, Inc., Biochemistry Department, Canoga Park, California 91303.
H M
HM
Said
A J
AJ
Feige
A E
AE
Newsom
S L
SL
Lauren
R A
RA
Mathews
D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005998:Glycine / Q000032:analysis*; D006197:Hair / Q000032:analysis*; D006801:Humans; D011506:Proteins / Q000302:isolation & purification*; D012967:Sodium Dodecyl Sulfate; D014443:Tyrosine / Q000032:analysis*
D000596:Amino Acids; D011506:Proteins; D012967:Sodium Dodecyl Sulfate; D014443:Tyrosine; D005998:Glycine