Related Experiment Video
Updated: Aug 29, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
Published on: September 20, 2012
Biochemical properties of black drum and sheepshead seabream skin collagen
Masahiro Ogawa1, Michael W Moody, Ralph J Portier
1Department of Food Science, Louisiana State University Agricultural Center, Baton Rouge, Louisiana 70803, USA.
Abstract:
Acid-soluble collagen (ASC) and pepsin solubilized collagen (PSC) were isolated from the skins of black drum (Pogonias cromis) and sheepshead seabream (Archosargus probatocephalus) harvested in the Gulf of Mexico coastal waters. The yields of ASCs on dry basis from black drum and sheepshead were estimated at 2.3 and 2.6%, and the yields of PSCs were 15.8 and 29.3%, respectively. Analyses of molecular weight profile, amino acid composition, and secondary structure showed that the skin collagens from both species were typical type-I collagen. The molecular mass of alpha(1) and alpha(2) subunits, as determined by SDS-PAGE using Tris-Acetate gels, was 127 kDa and 116 kDa, respectively. The amino acid composition of ASC and PSC for both species was closer to calf skin ASC than to cod skin ASC. Thermal denaturation temperatures, measured by melting point using circular dichroism, gave the following values: black drum ASC, 34.2 degrees C; sheepshead ASC, 34.0 degrees C; black drum PSC, 35.8 degrees C; sheepshead PSC, 34.3 degrees C. The literature value for the heat stability of calf skin collagen is 36.3 degrees C. The potentials of collagens from black drum and sheepshead skins in the functional food, healthcare, and pharmaceutical industries are discussed.
Related Concept Videos
Collagens are the Major Structural Proteins of ECM
Connective tissue proper includes loose...
Fibril-associated Collagen
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Connective Tissue Fibers and Ground Substance
Type IV Collagen of Basal Lamina
A type IV collagen molecule has six alpha chains which can exist in...
The Extracellular Matrix

