Physical Chemical Studies on Proteins and Polypeptides

Harrington, William F.; Josephs, R D; Segal, D M

doi:10.1146/annurev.bi.35.070166.003123

Cited by 71 publications

(20 citation statements)

References 77 publications

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“…Both samples showed a rotatory maximum at about 221 nm, a minimum at 193–196 nm, and a consistent crossover point (zero rotation) at about 212 nm. These spectral characteristics are typical of a collagen triple-helix structure [61,62,63]. The corresponding mean residue ellipticities, [ θ ] 221 , as a function of temperature, are shown in Figure 5C,D.…”

Section: Resultsmentioning

confidence: 94%

Collagen from the Marine Sponges Axinella cannabina and Suberites carnosus: Isolation and Morphological, Biochemical, and Biophysical Characterization

et al. 2017

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Abstract:In search of alternative and safer sources of collagen for biomedical applications, the marine demosponges Axinella cannabina and Suberites carnosus, collected from the Aegean and the Ionian Seas, respectively, were comparatively studied for their insoluble collagen, intercellular collagen, and spongin-like collagen content. The isolated collagenous materials were morphologically, physicochemically, and biophysically characterized. Using scanning electron microscopy and transmission electron microscopy the fibrous morphology of the isolated collagens was confirmed, whereas the amino acid analysis, in conjunction with infrared spectroscopy studies, verified the characteristic for the collagen amino acid profile and its secondary structure. Furthermore, the isoelectric point and thermal behavior were determined by titration and differential scanning calorimetry, in combination with circular dichroism spectroscopic studies, respectively.

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Section: Resultsmentioning

confidence: 94%

Collagen from the Marine Sponges Axinella cannabina and Suberites carnosus: Isolation and Morphological, Biochemical, and Biophysical Characterization

et al. 2017

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“…Figure shows the CD spectra of mmASC and mmPSC. It shows a rotator maximum at 221 nm, which is characteristic of the triple helical conformation of the collagen (Harrington, Josephs, & Segal, ; Heidemann & Roth, ). Although the peak patterns of both collagens were similar, the peak height of mmASC was higher than that of mmPSC.…”

Section: Discussionmentioning

confidence: 99%

Biochemical study of type I collagen purified from skin of warm sea teleost Mahi mahi ( Coryphaena hippurus ), with a focus on thermal and physical stability

Akita

Kono²,

Lloyd

et al. 2019

J Food Biochem

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Acid‐ and pepsin‐soluble collagen were purified from the skin of mahi mahi (mmASC and mmPSC). The Pro+Hyp content of the latter (185/1,000 residues) was highest among all marine teleost fishes. Fourier transform infrared spectroscopy and Circular Dichroism (CD) analysis showed the typical structure of type I collagen. The ratio of positive over negative peak intensity calculated from the CD spectrum was approximately 1.19 in mmPSC, which is remarkably high, and indicates the stability of the triple helix. The denaturation temperatures (Td) of mmASC and mmPSC were the highest (29.5 and 28.8°C, respectively) among the marine teleost fishes previously studied. atomic force microscope and scanning electron microscope images showed that even after pretreatment, the fibrils presented their structure and fiber orientation. These results indicate the robustness of both collagens, which can be attributed to the high value of Pro+Hyp stabilizing the helix structure of the collagen molecule. Practical applicationsWhile Mahi mahi is highly valuable for its meat, other parts such as skin is not fully utilized in seafood industry. On the contrary, it has been empirically shown that the skin of Mahi mahi has high thermal stability, thus, the skin has been used for leather products in some areas located in the tropical and subtropical zones. In this study, we focused on collagen a major component in skin and investigated the structure and the biochemical characteristics of it. Some results showed that collagen from skin has high physical stability. The collagen from skin of Mahi mahi will be a new fishery resource which could be used as a material for collagen products.

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“…1 shows the CD spectra of native and acylated collagens. Both native and acylated collagens displayed a weak positive maximum absorption band at 221 nm, a negative minimum absorption band at 198 nm and a cross over point (zero rotation) at about 214 nm, suggesting that the samples kept a typical triple helical conformation [26,27]. The results were similar to those of polyanionic collagen [25], but were different from those of gelatin and collagen hydrolysate, which showed the random coil configuration [12] and had no positive absorption peaks in CD spectra.…”

Section: Studiesmentioning

confidence: 99%

Structural properties of pepsin-solubilized collagen acylated by lauroyl chloride along with succinic anhydride

Tian

Liu

et al. 2015

Materials Science and Engineering: C

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Physical Chemical Studies on Proteins and Polypeptides

Cited by 71 publications

References 77 publications

Collagen from the Marine Sponges Axinella cannabina and Suberites carnosus: Isolation and Morphological, Biochemical, and Biophysical Characterization

Collagen from the Marine Sponges Axinella cannabina and Suberites carnosus: Isolation and Morphological, Biochemical, and Biophysical Characterization

Biochemical study of type I collagen purified from skin of warm sea teleost Mahi mahi ( Coryphaena hippurus ), with a focus on thermal and physical stability

Structural properties of pepsin-solubilized collagen acylated by lauroyl chloride along with succinic anhydride

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