Lactose intolerance is when the body does not produce enough lactase to break down lactose, a sugar found in milk and many other milk derived dairy products. The enzyme responsible for breaking down lactose is lactase, an enzyme found on the wall of the intestines. Lactase breaks down lactose (the sugar found in milk) into galactose and glucose. The activity of lactase becomes reduced after breastfeeding, at that point the body no longer needs as much lactase. Not to mention a human mothers milk is much different from the milk of a cow. The reduction of lactase activity after infancy is a genetically programmed event. Approximately 75 % of Earths population is lactose intolerant for a reason, that’s because it’s perfectly natural. The statistics vary from race to race and country to country but overall they show an abnormal amount of individuals who qualify. In some asian countries, 90 of the population is lactose intolerant. We are the only species on the planet that drinks milk from another species. Since lactase’s only function is the digestion of lactose in milk, most mammal species experience a dramatic reduction in the activity of the enzyme after weaning. Lactase persistence in humans has evolved as an adaptation to the consumption of non-human milk and dairy products consumed beyond infancy. Our diet has changed a lot, and as a result some of our genes have adapted, but it’s not an easy process. This is why most humans are lactose intolerant. Every other species weans and then never drinks milk again for the rest of their lives, and because of that we don’t have an enzyme to break down the sugar in milk. But during human evolution, some humans experienced a mutation in the LTC gene, the lactase gene, these mutations allow us to process lactose as adults. With over 75 percent of humans on the planet unable to properly process it, it is evidence enough that we are not doing what is natural and in accordance with our bodies. Our natural state is to be lactose intolerant. Undigested lactose in the small intestine acts like an osmotic agent, causing water and electrolytes to be pulled into the intestines, which results in diarrhea, bloating and gassiness. The body struggles and compensates, as well as protects itself by developing coping methods for our unnatural habits.
To reiterate, no other species on on the planet drinks the milk of another species except for humans and when animals do drink milk, they only consume it when they are babies. I’d like to say again that 75 percent of the planets population is lactose intolerant. It’s not hard to understand why milk can cause a huge number of health related issues. Animal cholesterol is the number one cause of heart disease as it destroys the inner lining of the arteries. This doesn’t allow the arteries to properly release a gas that is produced to break down cholesterol in the arteries. Eventually a build up happens and a heart attack is the result.
Currently there are movements occurring to try and remove milk from school cafeterias as a staple in children’s diet. Too much information is being released that disproves what was once believed about milk. A HUGE increase in milk alternative products like rice milk, almond milk and coconut milk are popping up in grocery stores and convenience stores everywhere. It seems it won’t be long before the truth about milk will become self evident. I strongly believe that the financial institutions that hold major stock in major food corporations are well aware that dairy products are harmful, and all of the injected advisee are not necessary. Milk is not needed, essential nutrients from milk are available in many other foods, like kale.
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Lactase enzyme, found in the cells lining the small intestine of mammals, cleaves lactose, a disaccharide, into the constituent monosaccharides, galactose and glucose, which are readily absorbed by the intestine. The amount of lactase activity decreases substantially after weaning in mammals, as lactose is no more a major part of their diet. This condition in humans is referred to as lactase non-persistence (LNP) or adult-type hypolactasia or primary lactose mal-digestion (LM). In several human societies all over the world, lactose is a part of the diet of adults due to the prevalence of dairy products and fresh milk in diet; this has been the case ever since human societies had domesticated cattle. A genetic mutation seems to have occurred in one (or more) such society (ies) resulting in lactase activity persisting in the cells lining the intestine even in adult stage. This condition is referred to as lactase persistence (LP). This mutation, due to its selective advantage, had spread extensively in such cattle rearing societies; this is the generally accepted explanation for Northern European societies having a large proportion (up to 90%) of the population being LP. Human genome sequencing studies done since 2001 have led to uncovering the molecular basis of this mutation. A single nucleotide polymorphism (SNP) at the position 13910 nucleotide upstream to the gene coding for lactase (LCT; located on chromosome 2) appears to determine the LP/LNP status of most populations studied. The nucleotide C at this position (which is the ancestral condition as determined by comparison with primate genome sequence data) corresponds to the LNP status whereas the nucleotide T at this position (which is a mutation) corresponds to the LP status. LP allele is dominant over LNP. This relationship between the SNP at -13910 upstream of LCT and LP/LNP has been verified for several populations including East Asia, East Europe etc and holds good nearly universally with the exception of some small pockets of indigenous populations in African Continent and Arabian peninsula. Studies carried out (to be published) in the Indian population by scientists at Biotools Technologies Pvt Ltd., and a Govt. Medical Research Laboratory show that the SNP at -13910 upstream of LCT does determine LP/LNP status in Indian population as well.