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Lactose intolerance is the ancestral state of all humans before the recent evolution of lactase persistence in some cultures, which extends lactose tolerance into adulthood. [9] Lactase persistence evolved in several populations independently, probably as an adaptation to the domestication of dairy animals around 10,000 years ago.
Lactase persistence or lactose tolerance is the continued activity of the lactase enzyme in adulthood, allowing the digestion of lactose in milk. In most mammals , the activity of the enzyme is dramatically reduced after weaning . [ 1 ]
Dual inheritance theory (DIT), also known as gene–culture coevolution or biocultural evolution, [1] was developed in the 1960s through early 1980s to explain how human behavior is a product of two different and interacting evolutionary processes: genetic evolution and cultural evolution.
Lactose intolerance is the inability to metabolize lactose, because of a lack of the required enzyme lactase in the digestive system. The normal mammalian condition is for the young of a species to experience reduced lactase production at the end of the weaning period (a species-specific length of time).
New results suggested that some adult Neanderthals were lactose intolerant. [9] On the question of potentially cloning a Neanderthal, Pääbo commented, "Starting from the DNA extracted from a fossil, it is and will remain impossible." [7] In May 2010, the project released a draft of their report on the sequenced Neanderthal genome.
Not all questions have simple, yes or no answers—including this one. While many dogs are lactose intolerant, many are not! Lactose intolerance develops as a dog grows up, so it can be impossible ...
Lactose intolerance is a condition in which people have symptoms due to deficiency or absence of the enzyme lactase in the small intestine, causing poor absorption of milk lactose. [ 123 ] [ 124 ] People affected vary in the amount of lactose they can tolerate before symptoms develop, [ 123 ] which may include abdominal pain, bloating ...
α-Lactalbumin forms the regulatory subunit of the lactose synthase (LS) heterodimer and β-1,4-galactosyltransferase (beta4Gal-T1) forms the catalytic component. Together, these proteins enable LS to produce lactose by transferring galactose moieties to glucose. As a multimer, α-lactalbumin strongly binds calcium and zinc ions and may possess ...