T mainly of two distinctive Thromboxane B2 custom synthesis varieties of -chains (1 and two) and dimeric -chains. The molecular weight of collagen was analyzed working with Quantity A single four.6.0 software program (Bio-Rad Laboratories, Hercules, CA, USA); we identified that the molecular weight of ASC (1-MW, 137 kDa; 2-MW, 127 kDa) was slightly higher than that of PSC (1-MW, 135 kDa; 2-MW, 123 kDa), which could be attributed towards the removal of telopeptide regions on the PSC . The protein patterns of ASC and PSC have been related to these of the collagen obtained from tilapia skin  and Pacific cod skin . Even though pepsin removed the cross-link-containing telopeptide, the electrophoresis patterns showed that PSC contained a higher intensity of -chains than ASC, indicating that PSC has higher molecular cross-linkages [23,24]. In addition, the ratio of 1 and two was calculated by Image J software (VERSION 1.eight.0, National Institute of Mental Wellness, Bethesda, MD, USA); especially, the ratios of 1 and two for ASC and PSC had been 1.86 and two.23, respectively, both close to 2:1, implying that ASC and PSC extracted from lizardfish scales are form I collagen (2 two) .Mar. Drugs 2021, 19, 597 Mar. Drugs 2021, 19, x FOR PEER Evaluation Mar. Drugs 2021, 19, x FOR PEER REVIEW3 of 17 three of 18 4 of2.three.3. Circular Dichroism (CD) Spectrum CD can be a simple and powerful strategy to determine whether the triple helical structure is intact . The CD spectrum of native collagen using a triplehelix structure shows a Etiocholanolone Epigenetics positive peak at 221 nm (maximum constructive cotton effect), a negative peak at 198 nm (max imum negative cotton effect), plus a crossover point (zero rotation) at about 213 nm [10,22]. As shown in Figure 2c, the CD spectrum of lizardfish scales ASC and PSC exhibited weak positive absorption peaks at 221 nm and 220 nm, respectively, and nega tive absorption peaks were observed at 198 nm and 197 nm, respectively, both with a crossover point at 213 nm. In addition, the Rpn values (the ratio on the positive to negative) of ASC and PSC have been 0.12 and 0.14, respectively, indicating that the collagen extracted from lizardfish scales possess a triplehelix conformation [26,27].Figure 1. SDSPAGE patterns of ASC and PSC from lizardfish scales. Lane 1: Marker typical; Lane Figure 1. SDS-PAGE patterns of ASC and PSC from lizardfish scales. Lane 1: Marker regular; 2: PSC; Lane 3: ASC. The experiment was carried out only after (n = 1). Lane two: PSC; Lane three: ASC. The experiment was carried out only when (n = 1). two.three.4. Xray Diffraction (XRD) Spectrum2.three.The XRD patterns of ASC and PSC are shown in Figure 2d. We identified that ASC and Spectroscopy Characterization two.three. Spectroscopy Characterization PSC consisted of two peaks, a sharp in addition to a broad peak. The diffraction angles (two) of ASC 2.three.1. UV Absorption Spectrum 2.3.1. UV Absorption Spectrum have been 7.86and 21.25 and these of PSC were 7.58and 21.02 that are constant with Frequently, collagen has a maximum absorption peak in 21040 nm variety, which can be Normally, collagen features a maximum absorption peak in 21040 nm range, which is the characteristic diffraction peaks of collagen . The d worth of the very first sharp peak of attributed to the presence of C=O, OOH, and CONH2 2groups within the polypeptide chains attributed for the presence of C=O, OOH, and CONH groups in the polypeptide chains ASC was 11.25 and that of PSC was 11.66 and this reflects the distance involving the of collagen . The UV absorption spectra of lizardfish scales coll.