Sequence analysis of <i>Camelus dromedarius</i> milk caseins

Kappeler, Stefan; Farah, Z.; Puhan, Z.

doi:10.1017/s0022029997002847

Cited by 139 publications

(183 citation statements)

References 18 publications

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“…Surprisingly, the situation is quite the opposite in the case of equine caseins, about which even less is known than caseins from different Camelidae [2,9,17,20,22,24].…”

Section: Introductionmentioning

confidence: 90%

“…* Les données concernant les caséines de vache, chèvre, souris et porc sont issues de la base de données Swissprot ; ¦ selon Ochirkhuyag et al [24] ; § selon Kappeler et al [17].…”

Section: Thermally Precipitated Casein Subfractionsunclassified

“…* Data on cow, goat, mouse and pig caseins are fiom the Swissprot database; ¦ according to Ochirkhuyag et al [24]; § according to Kappeler et al [17].…”

Section: Thermally Precipitated Casein Subfractionsmentioning

confidence: 99%

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Characterization of mare caseins. Identification of $\alpha_{{\bf S1}}$- and $\alpha_{{\bf S2}}$- caseins

Ochirkhuyag

Chobert²,

Dalgalarrondo³

et al. 2000

Lait

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-Whole mare (Mongolian and French breeds) casein was obtained from skim milk by isoelectric precipitation (pH 4.6) at 22 °C. In another series of experiments, equine caseins were fractionated after isoelectric precipitation at 4 °C, according to their sensitivity to temperature, on one hand, the pH of the resulting pellet was adjusted to 6.5 before centrifugation (45 000 g for 30 min) at 4 °C; on the resulting casein fraction which precipitated was named the cold precipitated (CP) fraction. On the other hand, the supernatant obtained from the centrifugation of skim milk at pH 4.6 and 4 °C was warmed to 30 °C before being centrifuged at 30 °C, 45 000 g, for 30 min. The resulting casein fraction which precipitated was named the thermally precipitated (TP) fraction. Equine caseins were then purified by high resolution gel chromatography on an anion-exchange column followed by reversed phase-high performance liquid chromatography. The casein fractions were analyzed by urea-and SDS-polyacrylamide gel electrophoresis, their amino acid compositions were determined and their first 15 N-terminal amino acids were sequenced. This analysis showed the presence of α slike caseins isolated from the CP fraction. α s1 -Like-casein showed 4 major double bands by electrofocusing with a pI range of 4.3-4.8. In the same conditions, α s2 -like casein showed 2 major bands with a pI range of 4.3-5.1. The TP fraction revealed the existence in equine milk of 6 subfractions of β-like caseins, occurring in the following ratios: 1:5:18:20:15:10, differing at least in their degree of phosphorylation (as shown also by the action of acid phosphatase). Since no evidence of the presence of κ-casein was found in equine milk, it is proposed that part of its functions in the milk of the Equidae could be assumed by the population of less phosphorylated β-caseins.

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“…Surprisingly, the situation is quite the opposite in the case of equine caseins, about which even less is known than caseins from different Camelidae [2,9,17,20,22,24].…”

Section: Introductionmentioning

confidence: 90%

“…* Les données concernant les caséines de vache, chèvre, souris et porc sont issues de la base de données Swissprot ; ¦ selon Ochirkhuyag et al [24] ; § selon Kappeler et al [17].…”

Section: Thermally Precipitated Casein Subfractionsunclassified

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Characterization of mare caseins. Identification of $\alpha_{{\bf S1}}$- and $\alpha_{{\bf S2}}$- caseins

Ochirkhuyag

Chobert²,

Dalgalarrondo³

et al. 2000

Lait

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“…Hypoallergenicity of mothers' milk was reported to be due to the high percentage of b-CN, low percentage of a-CN [28], deficiency of b-lactoglobulin [54] and similarity of the immunoglobulins [105]. It has been reported that camel milk could be a new protein source for children allergic to bovine milk.…”

Section: Camel Milk Safe For People Allergic To Bovine Milkmentioning

confidence: 99%

Camel Milk: An Important Natural Adjuvant

et al. 2017

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One humped camel (Camelus dromedarius) breeds, indigenous to India, have been shown to have good genetic potential to produce milk. Camel milk not only is cost-effective in terms of feed conversion but also has additional advantage of longer lactation period and unique adaptation mechanisms for warm arid and semiarid regions. The key features of camel milk in comparison with other milk are low fat with high content of unsaturated and long-chain fatty acid. The proteins are rich in lactoferrin and lysozymes, but deficient in b-lactoglobulin. It has higher percentage of total salts, free calcium, protective proteins and vitamin C, and some of the microminerals, viz iron, copper and zinc. Physicochemical properties of camel milk are also unique and useful for food processing. The shelf life of raw camel milk is 8-9 h, which can be extended up to 18-20 h through activation of camel lactoperoxidase system. Heat stability of camel milk is shown to be highest at pH 6.8, and it ferments relatively slowly compared to the cattle milk. The camel milk is successfully processed for producing a variety of products, such as fermented milk ('lassi'), soft cheese, flavored milk and 'kulfee' (a kind of ice cream). Camel milk has been traditionally used in different regions of the world as natural adjuvant for managing a variety of human diseases.

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“…CM's lactoferrin has very high levels of bactericidal and bacteriostatic properties against Gram-positive and Gram-negative bacteria (19), more than cow and human lactoferrin. CM contains various protective proteins, mainly enzymes which exert antibacterial and immunological properties (20). The fact that CM lacks β-lactoglobulin and a "new" β-casein (21), two powerful allergens in cow milk, makes the milk attractive for children suffering from milk allergies (22).…”

mentioning

confidence: 99%

Effect of camel milk on thymus and activation-regulated chemokine in autistic children: double-blind study

Bashir

Al-Ayadhi

2013

Pediatr Res

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Background: This study aimed to investigate the role of the effectiveness of camel milk (CM) (raw and boiled) on thymus and activation-regulated chemokine (TARC) serum levels and childhood autism rating scale (CARS) score in subjects with autism and compared to placebo group (cow milk). Methods: Forty-five subjects diagnosed with autism were randomly assigned to receive boiled CM for group I (n = 15), raw CM for group II (n = 15), and placebo for group III (n = 15) for 2 wk. Measures included changes in professionally completed CARS score and blood samples for TARC serum level were taken before and after milk consumption of 500 ml per day in children's regular daily diet. results: The serum levels of TARC decreased significantly (P = 0.004) in boiled CM and in raw CM group (P = 0.01) too, but no effect was observed (P = 0.68) in placebo group. Furthermore, significant improvements were observed in CARS score (P = 0.04) in raw CM group only. There were no significant relationships between the serum of TARC level and the CARS score, age, or gender for any group. conclusion: CM administered for 2 wk significantly improved clinical measurements of autism severity and decreased serum level of TARC in autistic children, but subsequent studies are recommended.

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Sequence analysis of Camelus dromedarius milk caseins

Cited by 139 publications

References 18 publications

Characterization of mare caseins. Identification of $\alpha_{{\bf S1}}$- and $\alpha_{{\bf S2}}$- caseins

Characterization of mare caseins. Identification of $\alpha_{{\bf S1}}$- and $\alpha_{{\bf S2}}$- caseins

Camel Milk: An Important Natural Adjuvant

Effect of camel milk on thymus and activation-regulated chemokine in autistic children: double-blind study

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