The Formation, Composition, and Properties of the Keratins

Ward, Wilfred H.; Lundgren, Harold P.

doi:10.1016/s0065-3233(08)60208-9

Cited by 99 publications

(21 citation statements)

References 61 publications

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“…The MW of epidermin is similar to the 47,000 to 68,000 value for prekeratin given by Denk et al (1979). The main component of epidermin has a MW around 60,000 (Kendrew 1954;Ward and Lundgren 1954). According to Denk et al (1979), antibodies to prekeratin of the 54,000 to 63,000 MW group show stronger reactions than antibodies to prekeratin with lower MW.…”

Section: Prekeratinsupporting

confidence: 69%

A comparative study of myosins and prekeratin in epithelial cells of methacarn-fixed tissues

et al. 1985

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Around the turn of the century, tonofibrils and contractile myofibrils were observed within the same cells. These findings have been largely forgotten. To clarify the topical relations of these proteins in epithelial cells, duplicate sections of methacarn-fixed human and canine tissues were treated with the tannic acid-phosphomolybdic acid (TP)-Levanol Fast Cyanine 5RN reaction for myosins and the PAP technic for prekeratin, respectively. In bronchi, lingual and sweat glands, liver and pancreas, myosin was confined to the terminal bar-terminal web system, including pericanalicular layers. Prekeratin occurred throughout the epithelium of bronchi and ducts; secretory cells showed little or no reaction. Observations on myosin in kidney confirmed data by Harper et al. (1970). The PAP technic colored transitional epithelium and collecting tubules intensely; convoluted tubules did not react. Staining of segments of Henle's loops varied from case to case. Both reactions colored thymic epithelial cells. In myoid cells of Hassall's corpuscles myosin was gradually replaced by prekeratin and keratin. Basal cells of epididymis reacted strongly with the PAP technic, but did not contain myosin. Prekeratin is apparently identical with epidermin, whose composition and structure were well known in the 1950's. Epidermin undergoes chemical changes as cells move from the stratum basale to the stratum corneum. According to DAKO, the antibodies used in this study were prepared with prekeratin extracted from stratum corneum. Data in the literature and observations in this investigation indicate that some samples of antibodies do not react with all tonofilaments.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Prekeratinsupporting

confidence: 69%

A comparative study of myosins and prekeratin in epithelial cells of methacarn-fixed tissues

et al. 1985

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“…5%) in comparison with other protein sources such as barley, oats and wheat. The low digestibility of feather protein is closely related to structural characteristics such as the relationship of β-sheet to solubility, keratin content and the disulfide bonding of the amino acids (Ward 1954;Fraser et al 1972;Greg and Rogers 1986;Chandler 2003). Our work (Yu et al 2004a) showed that feathers contained high β-sheet (88%) and low α-helix (4%), but the other protein sources with high protein nutritive value contained much less β-sheet and high α-helix, for example barley contained ca.…”

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confidence: 99%

Use of synchrotron-based FTIR microspectroscopy to determine protein secondary structures of raw and heat-treated brown and golden flaxseeds: A novel approach

Yu¹,

McKinnon²,

Soita³

et al. 2005

Can. J. Anim. Sci.

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. 2005. Use of synchrotron-based FTIR microspectroscopy to determine protein secondary structures of raw and heat-treated brown and golden flaxseeds: A novel approach. Can. J. Anim. Sci. 85: [437][438][439][440][441][442][443][444][445][446][447][448]. The objectives of the study were to use synchrotron Fourier transform infrared microspectroscopy (S-FTIR) as a novel approach to: (1) reveal ultra-structural chemical features of protein secondary structures of flaxseed tissues affected by variety (golden and brown) and heat processing (raw and roasted), and (2) quantify protein secondary structures using Gaussian and Lorentzian methods of multi-component peak modeling. By using multi-component peak modeling at protein amide I region of 1700-1620 cm -1 , the results showed that the golden flaxseed contained relatively higher percentage of α-helix (47.1 vs. 36.9%), lower percentage of β-sheet (37.2 vs. 46.3%) and higher (P < 0.05) ratio of α-helix to β-sheet than the brown flaxseed (1.3 vs. 0.8). The roasting reduced (P < 0.05) percentage of α-helix (from 47.1 to 36.1%), increased percentage of β-sheet (from 37.2 to 49.8%) and reduced α-helix to β-sheet ratio (1.3 to 0.7) of the golden flaxseed tissues. However, the roasting did not affect percentage and ratio of α-helix and β-sheet in the brown flaxseed tissue. No significant differences were found in quantification of protein secondary structures between Gaussian and Lorentzian methods. These results demonstrate the potential of highly spatially resolved S-FTIR to localize relatively pure protein in the tissue and reveal protein secondary structures at a cellular level. The results indicated relative differences in protein secondary structures between flaxseed varieties and differences in sensitivities of protein secondary structure to the heat processing. Further study is needed to understand the relationship between protein secondary structure and protein digestion and utilization of flaxseed and to investigate whether the changes in the relative amounts of protein secondary structures are primarily responsible for differences in protein availability. préciser l'ultrastructure chimique des structures secondaires des protéines du lin qu'affectent la variété (graines jaune pâle ou brunes) et le conditionnement thermique (graines naturelles ou grillées) et, d'autre part, (2) quantifier les structures secondaires en question par les méthodes de Gauss et de Lorenz de modélisation des pics multifactoriels. Quand on applique la modélisation des pics multifactoriels à la région de l'amide I des protéines (1 700-1 620 par cm), on constate que le lin jaune pâle se caractérise par une proportion relativement plus élevée d'hélices α (47,1 c. 36,9 %), une plus faible proportion de feuillets β (37,2 c. 46,3 %) et un ratio plus élevé (P < 0,05) entre hélices α et feuillets β (1,3 c. 0,8) que le lin brun. Le toastage réduit (P < 0,05) le pourcentage d'hélices α (de 47,1 à 36,1 %), augmente celui de feuillets β (de 37,2 à 49,8 %) et diminue le ratio entre hélices α et feuillets...

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“…Interestingly, hair concentrations of weak acids or neutral molecules (e.g., benzoylecgonine, THC) are generally less than the hair concentrations of weak bases (e.g., cocaine, nicotine, codeine), 1,6 and basic dyes have been shown to have a greater affinity for hair in comparison to acidic dyes. 14 Pigmentation is an important factor in determining drug incorporation into hair. [15][16][17] The accumulation of certain chemicals in pigmented tissues, due to melanin affinity, is a pronounced retention mechanism of the body.…”

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A Comparison of Phenobarbital and Codeine Incorporation into Pigmented and Nonpigmented Rat Hair

Gygi

Wilkins

Rollins

1997

Journal of Pharmaceutical Sciences

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Drugs and endogenous compounds circulating in the blood may ultimately become incorporated into a growing hair shaft. Hair analysis for drugs of abuse is a growing field in the area of forensic and clinical toxicology. However, the underlying principles that govern drug incorporation into hair are not known. In this study, we examined the incorporation of a weak acid, phenobarbital, and a weak base, codeine, into Sprague-Dawley (SD) rat hair. Codeine or phenobarbital was administered to male SD rats at 40 mg/kg/day for 5 days by intraperitoneal (ip) injection. Hair was collected from the back 14 days after beginning the 5-day dosing protocol and analyzed by gas chromatography/mass spectrometry (GC/MS) for codeine and phenobarbital. The time-courses of phenobarbital and codeine in plasma were also obtained after a single ip injection (40 mg/kg). Concentrations of codeine and phenobarbital in SD hair samples were 0.98 +/- 0.10 and 17.01 +/- 1.40 ng/mg hair. respectively. The areas under the curve (AUC) of plasma concentration versus time for codeine and phenobarbital were 1.58 and 414.50 micrograms h/microL, respectively. Notwithstanding the greater phenobarbital concentrations in hair, when plasma concentrations were considered, codeine was apparently incorporated to a 15-fold greater extent than phenobarbital. Because hair pigmentation may be important in drug incorporation, the incorporation of these two drugs was also studied in Long-Evans (LE; produces both black and white hair on the same animal) rats after 40 mg/kg/day of ip drug administration for 5 days. Hair was collected at the same time as the previous experiment. Concentrations of codeine in hair were 44-times greater in pigmented than nonpigmented hair from the same animals. In contrast, hair concentrations of phenobarbital were identical in both pigmented and nonpigmented hair. These data suggest that hair pigmentation greatly affects weak base incorporation but not weak acid incorporation into hair. Because hair concentrations of phenobarbital are not affected by pigmentation, phenobarbital may be an ideal drug to separate out factors other than pigmentation involved in incorporation of drugs into hair.

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The Formation, Composition, and Properties of the Keratins

Cited by 99 publications

References 61 publications

A comparative study of myosins and prekeratin in epithelial cells of methacarn-fixed tissues

A comparative study of myosins and prekeratin in epithelial cells of methacarn-fixed tissues

Use of synchrotron-based FTIR microspectroscopy to determine protein secondary structures of raw and heat-treated brown and golden flaxseeds: A novel approach

A Comparison of Phenobarbital and Codeine Incorporation into Pigmented and Nonpigmented Rat Hair

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