1984
DOI: 10.1017/s0016672300026227
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Protein and amino acid composition of hair from mice carrying the naked (N) gene

Abstract: The protein and amino acid compositions of hair from mice carrying the naked (N) gene were compared with those of wild-type (+ / + ) mouse hair using two-dimensional polyacrylamide gel electrophoresis and amino acid analysis. In samples obtained from N/ + mice, the numbers of positions of the low-sulphur (LS), high-sulphur (HS) and high tyrosine (HT) protein spots were indistinguishable from those observed in + / + samples but the amount of HT protein was reduced in N/ + hair. In samples obtained from N/N mice… Show more

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Cited by 11 publications
(5 citation statements)
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“…Hairs plucked from the dorsum were washed successively with ether, ethanol, water, and ethanol and air dried. Hair proteins were extracted essentially as described (Raphael et al, 1984). Briefly, approximately 10 mg of each hair sample was extracted for 5 h at room temperature under nitrogen with shaking in 8 M urea, 0.1 M dithiothreitol, 0.05 M Tris, pH 9.5, using 100 l solution per milligram of hair.…”
Section: Protein Analysis Of Hair Samplesmentioning
confidence: 99%
See 1 more Smart Citation
“…Hairs plucked from the dorsum were washed successively with ether, ethanol, water, and ethanol and air dried. Hair proteins were extracted essentially as described (Raphael et al, 1984). Briefly, approximately 10 mg of each hair sample was extracted for 5 h at room temperature under nitrogen with shaking in 8 M urea, 0.1 M dithiothreitol, 0.05 M Tris, pH 9.5, using 100 l solution per milligram of hair.…”
Section: Protein Analysis Of Hair Samplesmentioning
confidence: 99%
“…Extracts were spun in a benchtop microfuge to remove any insoluble material. The proteins in 100 l of each extract were S-carboxymethylated with iodo[2-14 C]acetic acid (53 mCi/mmol; Amersham) as described (Raphael et al, 1984). Equal numbers of TCA-precipitable counts for each sample were analyzed by two-dimensional gel electrophoresis according to the method of O'Farrell (1975) by Kendrick Labs, Inc. (Madison, WI) as follows.…”
Section: Protein Analysis Of Hair Samplesmentioning
confidence: 99%
“…7, 8, 160, 276 for detailed reviews). Some evidence exists suggt:sting that IF APs may also be involved directly or indirectly in diseases, especially in keratinizing disorders of hair (277,278) and skin (279,280) . Detailed studies will be required to understand the role of IFAPs in the organization of IF in both normal and abnormal cells.…”
Section: If-associated Proteinsmentioning
confidence: 99%
“…Thus, IF proteins are important markers of cell lineage and differentiation state and, moreover, are useful in the analysis of tumour cells which are known to retain and express the same IF complement as their parent cells (Osborn and Weber, 1983;Miettinen et al, 1984;Bolen and McNutt, 1987). Little is known about the involvement of IFAPs in the development of disease, although they have been implicated in keratinizing disorders of hair (Raphael et al, 1984) and skin (Dale et al, 1987).…”
Section: Immunochemical Propertiesmentioning
confidence: 99%
“…(i) Type I is made up of low molecular weight (10-45 kDa) molecules, as typified by filaggrin, which bind IFs laterally into tight macrofilament aggregates; (ii) higher molecular weight type II IFAPs (100-300 kDa), including paranemin, synemin, trichohyalin and plectin, which crosslink IFs into loose networks; (iii) type III includes proteins involved in coupling the ends of IFs to the plasma membrane and the nuclear lamina, such as ankyrin, spectrin and desmoplakin; and (iv) a number of proteins for which the association with the IF network is still unknown, e.g. Similarly IFAPs have also been implicated in disease states such as keratinizing disorders of hair (Raphael et al, 1984) and skin (Dale et al, 1987). Thus IF proteins are important markers for cell lineage and/or differentiation and aid in classifying cells of unknown origin occurring in malignant tumours.…”
Section: Introductionmentioning
confidence: 99%