journal article·1970-10

Amino Acid Composition of Human Hair

C.R. Robbins, C.H. Kelly

Textile Research Journal· Volume 40· Issue 10
Publisher page

Abstract

Samples of hair from five different female Caucasians were selected, while attempting to eliminate or minimize variables introduced by factors, suggested in previous literature, related to genetics, malnutrition, and cosmetic alteration, to analyze for 18 amino acids. The objective was to determine if human hair from such a similarly sampled group differs in composition from individual to individual. Significant differences were found for 9 of the 18 amino acids analyzed at the α = 0.01 level, however, the percent deviations for 16 of the amino acids were within ± 6%. Comparison of these samples of hair with pooled dark brown hair, from female Causasians, and purchased from a hair dealer, indicated a note-worthy difference only in the cystine content. Comparison of these data from human hair with that from 64's Merino wool indicates substantial differences between cystine, glycine, tyrosine, and phenylalanine. Statistically significant differences were suggested for other amino acids between Merino wool and human hair; however, the magnitude of the numerical differences, in these instances, was substantially lower than for the above mentioned four amino acids. Weathering effects in human hair were also explored, suggesting degradation to the amino acid residues of cystine, tyrosine, hysine, and histedine by the elements.
Source: crossref · Quality: baseline

Research context

OpenAlex topics: melanin and skin pigmentation · Skin Protection and Aging · Dyeing and Modifying Textile Fibers

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Colgate-Palmolive Co., River Road, Piscataway, New Jersey 08854, U. S. A.

References (24)

Show source-provided references
1. Bigwood, E.J. · Voeding · 1955 · 16 · 251
2. Block, R.J. · J. Biol. Chem. · 1939 · 128 · 18110.1016/S0021-9258(18)73740-X ↗
3. Block, R.J. · J. Soc. Cosmetic Chem. · 1951 · 4 · 235
4. 10.1021/ja01867a03010.1021/ja01867a030 ↗
5. 10.1042/bj059006210.1042/bj0590062 ↗
6. Gillespie, J.M. , The High-Sulfur Proteins of Normal and Aberrant Keratins, In "Biology of the Skin and Hair Growth," Proc. Canberra, Eds. Lynne and Short, 1964, pp. 377-398.
7. 10.6028/jres.017.05810.6028/jres.017.058 ↗
8. 10.1038/192457a010.1038/192457a0 ↗
9. Lang, J. · Biockem J. · 1952 · 52 · 84
10. 10.1177/00405175600300060810.1177/004051756003000608 ↗
11. Menkart, J. · J. Soc. Cosmetic Chem. · 1966 · 17 · 769
12. 10.1177/00405175700400051110.1177/004051757004000511 ↗
13. Noer, A. · nutrition · 1956 · 45 · 557
14. 10.1038/jid.1962.1610.1038/jid.1962.16 ↗
15. 10.1177/00405175670370091110.1177/004051756703700911 ↗
16. Robbins, C. · J. Soc. Cosmetic Chem. · 1969 · 20 · 555
17. 10.1177/00405175680380110510.1177/004051756803801105 ↗
18. 10.1071/BI954009810.1071/BI9540098 ↗
19. Simmonds, D.H.
20. 10.1177/00405175580280040410.1177/004051755802800404 ↗
21. Veldsman, D. · Wool Sci. Rev. · 1966 · 29 · 33
22. Ward, W.H. and Lundgren, H.P., The Formation, Composition and Properties of the Keratins, In " Advances in Protein Chemistry," Vol. IX, New York, Academic Press, 1954, p. 243.10.1016/S0065-3233(08)60208-9 ↗
23. Zahn, H. · J. Soc. Cosmetic Chem. · 1966 · 17 · 687
24. Zahn, H. · J. Soc. Cosmetic Chem. · 1963 · 14 · 529