Sequence of the goat αs2-casein-encoding cDNA

Bouniol, Christine

doi:10.1016/0378-1119(93)90336-2

Cited by 27 publications

(14 citation statements)

References 6 publications

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“…The α s2‐like caseins represent a more disparate group of highly phosphorylated peptides than the α s1‐caseins and have been identified from a number of eutherian species . As in the α s1‐caseins, the signal sequence is highly conserved but the mature proteins are quite divergent.…”

Section: Caseinsmentioning

confidence: 99%

“…34 The s2-like caseins represent a more disparate group of highly phosphorylated peptides than the s1-caseins and have been identified from a number of eutherian species. 9,35,36 As in the s1-caseins, the signal sequence is highly conserved but the mature proteins are quite divergent. s2-Casein (encoded by the CSN1S2 gene) has a polypeptide chain of 207 residues with a large number of positively charged side chains, especially in the C-terminal segment.…”

Section: S1-and S2-caseinsmentioning

confidence: 99%

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Investigating the genetic polymorphism of sheep milk proteins: a useful tool for dairy production

et al. 2014

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Sheep is the second most important dairy species after cow worldwide, and especially in the Mediterranean and Middle East regions. In some countries, the difficult environmental conditions require a peculiar adaptation and, in these contexts, sheep are able to provide higher quality protein than cattle. In the least-developed countries, the amount of dairy sheep and ovine milk production is progressively increasing. In order to improve dairy productions, in particular those with local connotations, it is necessary to obtain in-depth information regarding milk quality and rheological properties. The genetic polymorphisms of milk proteins are often associated with quantitative and qualitative parameters in milk and are potential candidate markers that should be included in breeding strategies similar to those already available for cattle. Due to the current and growing interest in this topic and considering the large amount of new information, the aim of this study was to review the literature on sheep milk protein polymorphisms with a particular emphasis on recent findings in order to give scientists useful support. Moreover, the effects of different protein variants on milk yield and composition are discussed.

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Section: Caseinsmentioning

confidence: 99%

Section: S1-and S2-caseinsmentioning

confidence: 99%

Investigating the genetic polymorphism of sheep milk proteins: a useful tool for dairy production

et al. 2014

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“…Comparison of primary structures of bovine, ovine and caprine κ-casein (a), β-casein (b), α s1 -casein (c) and α s2 -casein (d) (adapted from [4,5,34,41,43,58,61] [32], ovine and caprine caseinates [55] (Fig. 1d).…”

Section: Specificity Of Proteinases In Vitromentioning

confidence: 99%

Advances in the role of a plant coagulant (Cynara cardunculus) in vitro and during ripening of cheeses from several milk species

Sousa

Malcata

2002

Lait

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-Extracts from dried flowers of Cynara cardunculus have been employed successfully for many centuries in Portugal and some regions of Spain for the manufacture of traditional cheeses. Several studies have been performed in vitro and in actual cheeses focusing on the activity and specificity of proteinases from C. cardunculus, in attempts to further characterise this plant coagulant as a proteolytic agent in cheese ripening. In vitro studies encompassed extraction conditions, storage of extracts, proteolysis and specificity on caseins using experimental conditions that parallel milk and cheese during ripening. In vivo studies encompassed the effect of the type of milk (bovine, ovine and caprine) in terms of proteolysis, specificity of those plant proteinases during ripening, comparison of microbiological, chemical, proteolytic and lipolytic characteristics in ovine milk cheeses relative to animal rennet counterparts, and effect of native microflora, thermal processing and addition of starter cultures in ovine cheeses. milk clotting enzyme / plant coagulant / cheese / ewe's milk / cow's milk / goat's milk / ripeningResumé -Rôle de l'extrait coagulant de chardon (Cynara cardunculus) in vitro et au cours de l'affinage de fromages fabriqués à partir de laits de plusieurs espèces. L'extrait de fleurs séchées de Cynara cardunculus a été employé avec succès depuis plusieurs siècles au Portugal et dans quelques régions d'Espagne pour la fabrication de fromages traditionnels. De nombreuses études ont été réalisées in vitro et en fabrication fromagère sur l'activité et la spécificité des protéases de C. cardunculus, dans le but de mieux caractériser ce coagulant végétal comme agent protéolytique dans l'affinage du fromage. Les études in vitro ont concerné les conditions d'extraction, la conservation des extraits, la protéolyse et la spécificité sur les caséines en utilisant des conditions expérimentales qui 151

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“…However comparison of milk from the different ruminant species reveals great homologies in both protein composition and structure, particularly for the four caseins (a s 1 -, a s 2 -, b -, k -caseins) that are found in cow' s, sheep' s and goat' s milk, representing about 80% of milk proteins. Moreover im portant sequence conservation (between 80 and 90%) is observed for each of these caseins (Soulier et al, 1975;Richardson & Mercier, 1979;Boisnard & Petrissant, 1985, Brignon et al, 1989Provot et al, 1989;Roberts et al, 1992;Persuy et al, 1992;Bouniol, 1993). This could lead patients allergic to cow' s milk to express adverse reactions to milk from other ruminant species.…”

Section: Introductionmentioning

confidence: 91%

IgE Cross-reactivity with Caseins from Different Species in Humans Allergic to Cow's Milk

Bernard¹

1999

Food and Agricultural Immunology

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Fifty-eight sera from humans allergic to cow's milk proteins were analysed for the specificity of their IgE response to the whole casein fraction of milk from different ruminant and nonruminant species (e.g. cow, sheep, goat, rabbit and rat). IgE-specific responses were determined by an enzyme allergosorbent test using the purified casein fractions as immobilized antigen and an anti-human IgE monoclonal antibody labelled with acetylcholinesterase. Co-and/or cross-sensitizations to caseins of the different ruminant species occurred extensively, though IgE responses to ovine and caprine casein appeared to be lower than that obtained with bovine casein. Cross-reactivity is suggested by the significant reactivity of rat and rabbit casein toward human IgE. In terms of specificity and intensity, the IgE response to caseins demonstrates a great variability. Structural homologies in caseins of such different species, that can share common epitopes for the IgE of some patients, suggest that prevention of cow's milk allergy cannot be achieved by using milk from other species as substitutes.

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Sequence of the goat αs2-casein-encoding cDNA

Cited by 27 publications

References 6 publications

Investigating the genetic polymorphism of sheep milk proteins: a useful tool for dairy production

Investigating the genetic polymorphism of sheep milk proteins: a useful tool for dairy production

Advances in the role of a plant coagulant (Cynara cardunculus) in vitro and during ripening of cheeses from several milk species

IgE Cross-reactivity with Caseins from Different Species in Humans Allergic to Cow's Milk

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