Laser Raman Light-Scattering Observations of Conformational Changes in Myosin Induced by Inorganic Salts

Barrett, T. W.; Peticolas, Warner L.; Robson, Richard M.

doi:10.1016/s0006-3495(78)85454-x

Cited by 47 publications

(41 citation statements)

References 33 publications

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“…Some of these peaks have previously been associated with actin and myosin components of muscle tissue (Barrett et al . 1978; Carew et al . 1983; de Jong et al .…”

Section: Resultsmentioning

confidence: 99%

Label‐free Raman spectroscopic imaging to extract morphological and chemical information from a formalin‐fixed, paraffin‐embedded rat colon tissue section

Gaifulina

Maher

Kendall

et al. 2016

Int J Experimental Path

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SummaryAnimal models and archived human biobank tissues are useful resources for research in disease development, diagnostics and therapeutics. For the preservation of microscopic anatomical features and to facilitate long‐term storage, a majority of tissue samples are denatured by the chemical treatments required for fixation, paraffin embedding and subsequent deparaffinization. These aggressive chemical processes are thought to modify the biochemical composition of the sample and potentially compromise reliable spectroscopic examination useful for the diagnosis or biomarking. As a result, spectroscopy is often conducted on fresh/frozen samples. In this study, we provide an extensive characterization of the biochemical signals remaining in processed samples (formalin fixation and paraffin embedding, FFPE) and especially those originating from the anatomical layers of a healthy rat colon. The application of chemometric analytical methods (unsupervised and supervised) was shown to eliminate the need for tissue staining and easily revealed microscopic features consistent with goblet cells and the dense populations of cells within the mucosa, principally via strong nucleic acid signals. We were also able to identify the collagenous submucosa‐ and serosa‐ as well as the muscle‐associated signals from the muscular regions and blood vessels. Applying linear regression analysis to the data, we were able to corroborate this initial assignment of cell and tissue types by confirming the biological origin of each layer by reference to a subset of authentic biomolecular standards. Our results demonstrate the potential of using label‐free Raman microspectroscopy to obtain superior imaging contrast in FFPE sections when compared directly to conventional haematoxylin and eosin (H&E) staining.

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“…Some of these peaks have previously been associated with actin and myosin components of muscle tissue (Barrett et al . 1978; Carew et al . 1983; de Jong et al .…”

Section: Resultsmentioning

confidence: 99%

Label‐free Raman spectroscopic imaging to extract morphological and chemical information from a formalin‐fixed, paraffin‐embedded rat colon tissue section

Gaifulina

Maher

Kendall

et al. 2016

Int J Experimental Path

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“…183 -189 Changes in secondary structural conformation of rabbit myosin induced by low concentrations of inorganic salts were investigated by an analysis of bands at 900, 940, 1240-1300 and 1650-1670 cm 1 . 184 A helix-to-sheet transition was observed in the presence of CaCl 2 , whereas LiBr appeared to denature the protein leading to increased random coil; MgCl 2 had an effect intermediate between those of CaCl 2 and LiBr. The effects of Mg 2C , ATP and Ca 2C on muscle contraction of internally perfused barnacle muscle fibers showed strong interactions between basic and acidic residues during contraction and a change of the helical content or orientation of some of the contractile proteins.…”

Section: Handbook Of Vibrationalmentioning

confidence: 94%

Vibrational Spectroscopy of Food and Food Products

Li‐Chan¹,

Ismail²,

Sedman³

et al. 2001

Handbook of Vibrational Spectroscopy

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Vibrational spectroscopy may be applied to the qualitative and quantitative analysis of complex food systems. Mid infrared (MIR) spectroscopy and Raman spectroscopy are valuable tools for identification and structural characterization of food components and for elucidating structure–function relation of food biopolymers such as proteins. Fourier transform infrared(FT‐IR) spectrometers and chemometrics have broadened the scope of MIR spectroscopy for quality control analysis, but such applications remain generally limited to homogeneous fluid products such as beverages, juices, fats, and oils. In contrast, near infrared (NIR) and FT‐NIR spectroscopy in conjunction with multivariate calibration techniques is becoming increasingly popular in the food industry for rapid and routine analysis of proximate composition of various foods as well as for authentication and detection of adulteration. Increasing application of Raman spectroscopy in food analysis is expected with recent developments in NIR‐FT Raman spectrometers, fibre optic sampling, and confocal Raman microscopy.

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“…This technique has been used to study the sub-structure ofmyosin (Carew et al, 1975) and the effects of inorganic salts on myosin solutions (Barrett and Peticolas, 1978).…”

Section: Infrared Spectroscopymentioning

confidence: 99%

Protein Structural Changes During Preparation and Storage of Surimi

Moosavi‐Nasab

Alli

Ismail

et al. 2005

Journal of Food Science

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: The changes in protein structure associated with the preparation and frozen storage of surimi were investigated. Raw surimi was prepared by repeatedly washing Alaska pollock flesh with chilled water. The product was either slowly frozen or underwent rapid freezing using liquid air; in either case it was then subjected to frozen storage at ‐20 °C for 24 mo. Fourier transform infrared/attenuated total reflectance (FTIR/ATR) spectroscopy showed that during preparation of surimi, the a‐helix content increased with increased number of washing cycles. Differential scanning calorimetry (DSC) revealed a shift in the thermal transition of actin to a higher temperature during surimi preparation. Electrophoresis, FTIR/ATR spectroscopy, and DSC results revealed a loss of myofibrillar proteins from surimi after 3 washing cycles, suggesting that 3 washing cycles were adequate to prepare surimi. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) showed relatively minor changes in protein subunit structure with some loss of the myosin light chains (MLC); myosin heavy chain (MHC), actin, and tropomyosin were found to be relatively stable. Native‐PAGE showed no major changes in surimi after 24 mo storage at ‐20 °C. FTIR/ ATR spectroscopy indicated a significant decrease in a‐helix relative to p‐sheet structure in surimi after 2 y of storage at ‐20 °C. The loss of α‐helical content was more significant in slowly frozen surimi compared with rapid‐frozen surimi samples. DSC results revealed a shift in the thermal transition of actin to lower temperatures during frozen storage of surimi.

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Laser Raman Light-Scattering Observations of Conformational Changes in Myosin Induced by Inorganic Salts

Cited by 47 publications

References 33 publications

Label‐free Raman spectroscopic imaging to extract morphological and chemical information from a formalin‐fixed, paraffin‐embedded rat colon tissue section

Label‐free Raman spectroscopic imaging to extract morphological and chemical information from a formalin‐fixed, paraffin‐embedded rat colon tissue section

Vibrational Spectroscopy of Food and Food Products

Protein Structural Changes During Preparation and Storage of Surimi

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