Comparison of the nucleotide sequence of cloned human and guinea-pig pre-α-lactalbumin cDNA with that of chick pre-lysozyme cDNA suggests evolution from a common ancestral gene

Abstract

Nucleotide sequence analyses of essentially full-length copies of human and guinea-pig pre-alpha-lactalbumin cDNAs contained within recombinant plasmids, (i) confirm the presence of 19 amino acid hydrophobic amino terminal peptide extensions encoded within each mRNA; and (ii) provides evidence for the existence of a minor variant of guinea-pig alpha-lactalbumin mRNA encoding a protein with a 36 residue carboxyl-terminal extension. Comparison of the nucleotide sequence within the coding region of the human, and the predominant guinea-pig pre-alpha-lactalbumin mRNAs, with the analogous region of hen pre-lysozyme mRNA provides compelling evidence that all have evolved from a common ancestral gene.

Molecular cloning and analysis of four potato tuber mRNAs

“…On the other hand comparison of the amino terminal (Nterminal) amino acid sequence to published protein sequences showed homology to some of these. Starting at the methionine residue mentioned the p322 polypeptide showed 54% identity to the N-terminal part of the signal peptide of human lactalbumin precursor protein [14] (7 out of 13 N-terminal amino acids), suggesting the presence of a signal peptide in the N-terminal domain of p322. This was further supported by the presence of the amino acid sequence phe-phe-leu-leu-ala (nucleotides 25 to 40) also found in the signal peptide of the proteinase inhibitor I of potato ( [4], W. J. Stiekema, unpublished results).…”

Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes: Calcium-binding lysozymes and their relationship with α-lactalbumins

“…(t) Echidna milk I (Tachyglossus aculeatus multiaculeatus) (Teahan et al, 1991). b ol-Lactalbumins: (h) Human milk (Homo sapiens) (Findlay and Brew, 1972, with corrections from Hall et al, 1982). (c) Cow milk (Variant B) (Bos (bos)) Vanaman et al, 1970;Shewale et al, 1984;note Vilotte et al (1987) obtain Gin, Asp, Asn for residues 39, 63, 66, respectively, from nucleotide sequence.…”

“…However, there is no uncertainty in the sequence of human crlactalbumin (Hall et al, 1982). It is reassuring that its three-dimensional structure has now been determined at 1.7A resolution (Acharya et al,199l) and it is closely similar to that of baboon milk o~-lactalbumin.…”

Physicochimie et biochimie des protéines du lait. Données récentes

“…Sont connues les structures primaires des 6 protéines bovines majeures (les 4 caséines, l'a-lactalbumine -oel.a, la~-lactoglobuline -~Lg) (Swaisgood, 1982;et corrections dans Ribadeau-Dumas, 1988), de la butyrophiline (Jack et Matter, 1990) et des lactoperoxidases bovine et humaine (Dull et al, 1990;Cals et al, 1990); des 2 caséines humaines (~et K) (Brignon et al, 1985;l.ônnerdal et al, 1990), de l'alactalbumine (Hall et al, 1982), de la lacteferrine (Powell et Ogden, 1990;Rey et al, 1990) et du lysozyme (Canfield et al, 1971;Jollès et Jollès, 1971) humains. Sont connues également les structures tridimensionnelles de l'a-lactalbumine de babouin très voisine de la protéine humaine (Acharya et al, 1989), de la~-Iactoglobuline bovine (Papiz et al, 1986;Monaco et al, 1987), du lysozyme et de la lactoferrine (Anderson et al, 1989) humains.…”