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New-born mammals

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New-born mammals

Postby ropeyboy » Wed Apr 11, 2007 8:46 pm

can anyone give me an answer for this?

New-born mammals do not produce trypsin and their stomachs do not secrete hydrochloric acid. explain how these features enable intestines of new-born mammals to absorb proteins??

thnx for any replies
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Postby Dr.Stein » Thu Apr 12, 2007 3:47 am

Newborn mammals got protein from milk (casein), which the proper enzyme for its digestion is lactase :)
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Postby Darby » Thu Apr 12, 2007 3:25 pm

Hydrochloric acid is primarily to separate out complex, fibrous materials, and to denature a wide range of proteins.

Milk has just a few proteins. The main one, albumin (the same one stored in egg whites, more-or-less), denatures fairly easily, so the HCl and pepsin of the stomach isn't needed.

I have to disagree with Dr. Stein - lactase is for digesting lactose, which is a carbohydrate, not a protein. Trypsin is involved in casein digestion (but I'm not sure it's essential.

Anyway, a quick literature search online would seem to indicate that your premise is partly flawed - there are lots of studies involving trypsin levels in neonates, and they all expected it to be there. I didn't check on HCl, but I wonder about the reliability of your source.
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Postby CoffeaRobusta » Fri Apr 13, 2007 6:20 am

Yeah, I was thinking the question is worded wrong. I searched for trypsin and found a lot of studies looking at it in newborns. In addition, it seems that trypsin works best in a slightly alkaline environment.
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Postby Dr.Stein » Fri Apr 13, 2007 6:28 am

Darby wrote:I have to disagree with Dr. Stein - lactase is for digesting lactose, which is a carbohydrate, not a protein. Trypsin is involved in casein digestion (but I'm not sure it's essential

Oops sorry, I got rush in my mind. The product of milk digestion is lactose, which needs lactase but that's not the idea. Well, enzyme to deal with casein is chymosin/rennin. Sorry :oops:
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Postby arian » Wed Apr 18, 2007 11:15 am

Trypsins can be used to breakdown casein in breast milk. If trypsin is added to a solution of milk powder, the breakdown of casein will cause the milk to become translucent. The rate of reaction can be measured by using the amount of time it takes for the milk to turn translucent.

Trypsin can also be used to dissociate dissected cells. For example, prior to cell fixing and sorting.

Trypsin is commonly used in proteomics experiments to digest and make proteins into peptides. Trypsin is particularly suited for this, since it has a very well defined specificity.

Trypsin can also be used to dissolve blood clots in its microbial form and treat inflammation in its pancreatic form.

Trypsin is used in baby food to pre-digest it. It can break down the protein molecules which helps the baby to digest it as its stomach is not strong enough to digest bigger protein molecules
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Postby Sillitovet » Fri May 04, 2007 8:45 pm

Could the question be referring to the fact that many new born mammals absord immunoglobulins directly across the intestine for the first few hours of life? If there was no HCL early on I suppose that would stop them getting denatured and ruined.
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