Characterization of a heterogeneous camel milk whey non‐casein protein

Abstract

A milk protein, occurring in the whey fraction, has been characterized from camel milk. Determination of the primary structure reveals the existence of two related types of chain with residue differences in at least the N-terminal region. A fragment representing an N-terminal part of the protein was also recovered (heterogeneous at the same positions). The absence of cysteine residues in the protein shows that no disulphide bridges are present. The pattern of fragments and a parent protein resembles that for casein and its fragments, showing that fragments and a multiplicity of forms may be typical for different milk proteins.

Separation and characterization of major milk proteins from Algerian<br>Dromedary (Camelus dromedarius)

“…Camel whey proteins were separated into 3 fractions. As observed by native-PAGE (Figure 4), serum albumin was eluted in fraction1, the two forms of α-lactalbumin were eluted in fraction 2 and the third peak contained no identified proteins which could correspond to heterogeneous camel milk whey proteins (Beg et al, 1987). It is assumed that other whey components such as lactoferrine (75-76 kDa), lactoperoxydase (69 kDa) and the 43 kDa fraction (Kappeler, 1998) will not be separated on the columns used in this work.…”

Compositional, technological and nutritional aspects of dromedary camel milk

“…Camel milk a-lactalbumin was reported to have a molecular mass of 14.6 kDa and to comprise 123 residues, which is similar to bovine, human and goat milk a-lactalbumin (Beg, 1986;Beg, BahrLindström, Zaidi, & Jörnvall, 1985). However, SDS-PAGE results show that human whey proteins are characterized by the presence of high intensity a-lactalbumin and lactoferrin bands, whereas, alactalbumin and blood serum albumin (BSA) bands are dominant in camel whey proteins (El-Agamy et al, 2009).…”

Human insulin‐like growth‐factor‐binding protein

“…This protein polymorphism corresponds to a onebase variation, probably of allelic origin, compatible with the Thus, this region is possibly exposed on the surface of the mature binding protein. A compact Cys-rich structure has also been demonstrated for other binding proteins [30]. Although such Cys patterns often do not show sequence similarities…”

“…apart from the relative abundance of half-cystines, the possibility of forming a tightly folded structure is a characteristic property of several binding proteins [30]. Considering the extracellular location of the IGF-binding protein, it is an interesting observation that this protein has the amimo acid sequence RGD at positions 221 -223.…”