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Lactalbumin, alpha-, also known as LALBA, is a protein which in humans is encoded by the LALBA gene



a-lactalbumin is an important whey protein in cow's milk (~1 g/l), and is also present in the milk of many other mammalian species. In primates, alpha-lactalbumin expression is upregulated in response to the hormone prolactin and increases the production of lactose.[4]



a-lactalbumin forms the regulatory subunit of the lactose synthase (LS) heterodimer and ß-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 monomer, alpha-lactalbumin strongly binds calcium and zinc ions and may possess bactericidal or antitumor activity. A folding variant of alpha-lactalbumin, called HAMLET, likely induces apoptosis in tumor and immature cells.[1]



When formed into a complex with Gal-T1, a galactosyltransferase, a-lactalbumin enhances the enzyme's affinity for glucose by about 1000 times, and inhibits the ability to polymerise multiple galactose units. This gives rise to a pathway for forming lactose by converting Gal-TI to Lactose synthase.

Glycomacropeptides (GMP): Whey protein is obtained from milk from one of the initial steps in the process of making cheese. During this process, one of the milk proteins, called casein (kappa casein) is split. GMP is the resulting composition of a certain amino acid sequence from this product. GMP supplementation has been shown to increase levels of cholecystokinin, a stomach secretion that plays a role in regulating feelings of fullness. GMP also may help to prevent dental cavities, and protect against viruses and bacteria.

Immunoglobulins, or antibodies, are a complex, heterogeneous mixture of proteins that exhibit two fundamental types of structural variation. Subtle structural differences in their antigen combining sites, or variable regions, account for their unique antigen binding specificities (see Figure 4-3). Structural differences outside their antigen combining sites, in the so-called constant regions, correlate with the different effector functions mediated by antibodies, such as complement activation or binding to one or more of the antibody Fc receptors expressed on monocytes and granulocytes.

Antibody proteins are often called immunoglobulins ( Ig). All immunoglobulin molecules have many common structural features…The antibodies are made of protein "chains" linked together by chemical bonds. There are "heavy" chains and "light" chains. I will spare you the intricacies of the detailed description of these chains



Source:http://www.lymphomation.org/tests-immunoglobulins.htm

Lactoperoxidase is an enzyme extracted from premium quality bovine milk. It has been shown to be bacteriostatic against gram-positive organisms and exhibits pH dependent bacteriocidal action against gram-negative organisms in the presence of thiocyanate and hydrogen peroxide. Lactoperoxidase offers the following benefits:

Relaxin is a protein hormone first described in 1926 by Frederick Hisaw.[1][2]



The relaxin-like peptide family belongs in the insulin superfamily and consists of 7 peptides of high structural but low sequence similarity; relaxin-1 (RLN1), 2 (RLN2) and 3 (RLN3), and the insulin-like (INSL) peptides, INSL3, INSL4, INSL5 and INSL6. The functions of relaxin-3, INSL4, INSL5, INSL6 remain uncharacterised.[3]



Contents [hide]

1 Synthesis

2 Structure

3 Function

3.1 In humans

3.2 In other animals

4 Receptors

5 Disorders

6 References

7 External links



[edit] SynthesisIn the female, it is produced by the corpus luteum of the ovary, the breast and, during pregnancy, also by the placenta, chorion, and decidua.



In the male, it is produced in the prostate and is present in human semen.[4]



[edit] StructureSee also: Insulin/IGF/Relaxin family

Structurally, relaxin is a heterodimer of two peptide chains of 24 and 29 amino acids linked by disulfide bridges, and it appears related to insulin.



Relaxin is produced from its prohormone, “prorelaxin”, by splitting off one additional peptide chain.



[edit] Function[edit] In humansIn males, relaxin enhances motility of sperm in semen.[5] In females relaxin is produced mainly by the corpus luteum, in both pregnant and nonpregnant females; it rises to a peak within approximately 14 days of ovulation, and then declines in the absence of pregnancy, resulting in menstruation. During the first trimester of pregnancy, levels rise and additional relaxin is produced by the decidua.



Relaxin's role or necessity in human pregnancy remains under investigation, as in humans its peak is reached during the 14 weeks of the first trimester and at delivery. It is believed to soften the pubic symphysis.



[edit] In other animalsIn animals, relaxin widens the pubic bone and facilitates labor; it also softens the cervix (cervical ripening), and relaxes the uterine musculature. Thus, for a long time, relaxin was looked at as a pregnancy hormone. However, its significance may reach much further. Relaxin affects collagen metabolism, inhibiting collagen synthesis and enhancing its breakdown by increasing matrix metalloproteinases.[6] It also enhances angiogenesis and is a potent renal vasodilator.



[edit] ReceptorsRelaxin interacts with the relaxin receptor LGR7 (RXFP1) and LGR8 (RXFP2), which belong to the G protein-coupled receptor superfamily [7]. They contain a heptahelical transmembrane domain and a large glycosylated ectodomain, distantly related to the receptors for the glycoproteohormones, such as the LH-receptor or FSH-receptor.



Relaxin receptors have been found in the heart, smooth muscle, the connective tissue, and central and autonomous nervous system.



[edit] DisordersSpecific disorders related to relaxin have not been described, yet a link to scleroderma and fibromyalgia has been suggested.[8]

ß2 microglobulin also known as B2M is a component of MHC class I molecules, which are present on all nucleated cells (excludes red blood cells).[1][2] In humans, the ß2 microglobulin protein[3] is encoded by the B2M gene.[2][4]



Contents [hide]

1 Structure and function

2 Clinical significance

3 References

4 Further reading

5 External links



[edit] Structure and function

Schematic representation of MHC class Iß2 microglobulin lies lateral to the a3 chain on the cell surface. Unlike a3, ß2 has no transmembrane region. Directly above ß2 (i.e. away from the cell) lies the a1 chain, which itself is lateral to the a2.



ß2 microglobulin associates not only with the alpha chain of MHC class I molecules, but also with class I-like molecules such as CD1 and Qa[disambiguation needed ].



An additional function is association with the HFE protein, together regulating endocytosis of iron into intestinal cells. Loss of this function causes iron excess and hemochromatosis.



[edit] Clinical significanceIn patients on long-term hemodialysis, it can aggregate into amyloid fibers that deposit in joint spaces, a disease known as dialysis-related amyloidosis.



Mice models deficient for the ß2 microglobulin gene have been engineered. These mice demonstrate that ß2 microglobulin is necessary for cell surface expression of MHC class I and stability of the peptide binding groove. In fact, in the absence of ß2 microglobulin, very limited amounts of MHC class I (classical and non-classical) molecules can be detected on the surface. In the absence of MHC class I, CD8 T cells cannot develop. (CD8 T cells are a subset of T cells involved in the development of acquired immunity.)Low levels of ß2 microglobulin can indicate non-progression of HIV.



Levels of beta-2 microglobulin can be elevated in multiple myeloma and lymphoma,[5] though in these cases primary amyloidosis (amyloid light chain) and secondary amyloidosis (Amyloid associated protein) are more common. the normal value of beta-2 microglobulin ranges from( 1 - 2.1 )

A colorless, crystalline organic compound belonging to the family of carboxylic acids, present in practically all plants and in many animal tissues and fluids. It is one of a series of compounds involved in the physiological oxidation of fats, proteins, and carbohydrates to carbon dioxide and water.



First isolated from lemon juice by a Swedish chemist, Carl Wilhelm Scheele, in 1784, citric acid is manufactured by fermentation of cane sugar or molasses in the presence of a fungus, Aspergillus niger. It is used in confections and soft drinks (as a flavoring agent), in metal-cleaning compositions, and in improving the stability of foods and other organic substances (by suppressing the deleterious action of dissolved metal salts)."



Citrus fruits are notable for their fragrance, and most are juice-laden. They contain a high proportion of citric acid giving them their characteristic astringent odour and flavour. They are also good sources of vitamin C. In botanical terms, "The fruit of all Citrus trees, in which the true fruit is the peel, [is] made up of an outer layer, brightly colored and rich in glands, a spongey whitish mesocarp, and a membraneous endocarp surrounding the segments. The succulent parts we eat is only a secondary tissue developed as a filler"



List of citrus fruits:

Amanatsu

Bergamot orange

Bitter orange (Seville Orange)

Calamondin (Calamansi)

Citron

Clementine

Golden Lime - hybrid between the genus Citrus and the genus Fortunella

Daidai

Dancy

Grapefruit

Ichang Lemon

Iyokan

Kaffir lime

Key lime

Kumquat - in the related genus Fortunella, not Citrus; forms hybrids with Citrus

Lemon

Lime

Limequat

Mandarin Lime

Mandarin Orange

Meyer Lemon

Mikan

Minneola

Natsumikan

Orange

Orangelo (Chironja)

Orangequat

Persian lime (Tahiti lime)

Pomelo (Pummelo, Shaddock)

Ponkan

Rangpur (Lemanderin)

Rough Lemon

Satsuma

Shekwasha (Taiwan Tangerine)

Sudachi

Sweetie

Tachibana Orange

Tangelo

Tangerine

Tangor

Ugli

Yuzu



Some brands of Citric Acid may be made from wheat, however this is very rare.

Flavor(s) Natural & Artificial

A combination of both what is considered “natural” and “artificial” flavoring under the Federal Drug Administration(FDA) Regulations. Artificial flavoring “means any substance, the function of which is to impart flavor, which is not derived from a spice, fruit or fruit juice, vegetable or vegetable juice, edible yeast, herb, bark, bud, root, leaf or similar plant material, meat, fish, poultry, eggs, dairy products, or fermentation products thereof.” In other words, substances not found in nature to add flavor to a substance is considered artificial. See Artificial Flavor. Natural flavoring “means the essential oil, oleoresin, essence or extractive, protein hydrolysate, distillate, or any product of roasting, heating or enzymolysis, which contains the flavoring constituents derived from a spice, fruit or fruit juice, vegetable or vegetable juice, edible yeast, herb, bark, bud, root, leaf or similar plant material, meat, seafood, poultry, eggs, dairy products, or fermentation products thereof, whose significant function in food is flavoring rather than nutritional.” See Natural Flavor.

Code of Federal Regulations Title 21 of the Us. Food and Drug Administration. Title 21. Volume 2. Revised 1 April 2010.

Lecithin: Used to stabilize emulsions;

Lecithin is present in all living cells and is a significant constituent of nerve and brain cells.



Commercial lecithin, most of which comes from soya bean oil, which may be Genetically Modified, contains a mixture of phosphoglycerides containing principally lecithin, cephalin and phosphatidyl inositol. Other sources are egg yolk, from where it was originally obtained, and leguminous seeds, including peanuts and maize, which also may be Genetically Modified. Vegetarians should be aware that it can also be obtained from animal fat.

Natural food enzymes that, when taken with gassy foods, help reduce flatulence-sometimes even stopping it before it begins. Gas-producing foods like beans, broccoli, cabbage, cauliflower, grains and onions cause trouble because they contain hard- or impossible-to-digest complex sugars (see CARBOHYDRATE) that ferment in the large intestine. Digestive enzymes help break down these complex sugars into simple sugars that are more easily digestible.



Proteins produced by the cells that are crucial in chemical reactions and in building up or synthesizing most compounds in the body. Each enzyme has a specific function. The two classes of enzymes are metabolic and digestive. Metabolic enzymes catalyze the many chemical reactions in the body. Digestive enzymes are responsible for breaking down food into smaller absorbable units. There are specific enzymes that break down protein, fat and carbohydrate; these are protease, amylase and lipase respectively.

Acesulfame Potassium

Also seen as Acesulfame K, Ace-K, Sunett, or Sweet One, Acesulfame Potassium is a sugar substitute that is 200 times sweeter than table sugar. It is used as a flavor enhancer and sweetener for foods. It is a low calorie food ingredient because our bodies do not metabolize it. Acesulfame K also is not consumed by bacteria so it does not contribute to tooth decay as sugar does. However, methylene chloride is used for the production of Acesulfame K, which also is used as a propellant, degreaser, and paint stripper. There are many side effects with consumption of Acesulfame K, including increased risk for cancer, triggering chronic respiratory disease, or abnormal cravings for sweets. The chemical remains stable when exposed to heat, basic, or acidic conditions. Since it is stable under high heat, manufacturers use Acesulfame K potassium to use in baking and extending shelf life. This artificial sweetener has a slight bitter aftertaste, but companies are using this with sodium ferulate to mask the bitterness. Other companies use Acesulfame K with other alternative sweeteners such as Aspartame or sucralose to control the use of it. The Food and Drug Administration (FDA) recommends the acceptable daily intake of 15mg/kg of body weight/day.

"Artificial Sweeteners Symptoms, Causes, Treatment - Acesulfame K: What Are the Pros on

MedicineNet." Web. 17 May 2011. .

Denby, Amelia. "Acesulfame Potassium Dangers Medical Questions, Weight Loss, Pregnancy, Drugs,

Health Insurance." Health: Medical Questions, Weight Loss, Pregnancy, Drugs, Health Insurance. 14 Jan. 2011. Web. 17 May 2011. .

"What Is Acesulfame Potassium?" Tech-FAQ. Web. 17 May 2011.
faq.com/acesulfame-potassium.html>.

Approved in the United States in April 1998, sucralose (a synthetic chemical) can be used in soft drinks, baked goods, ice cream, sweetener packets, and other products. It previously had been used in Canada, Europe, and elsewhere. Sucralose is safer than saccharin and cyclamate and doesn’t raise the concerns that tests on acesulfame-K and aspartame have raised.

Red 40

Red 40 is a dye commonly used as food coloring in today’s foods. The proper chemical name is actually

6-hydroxy-5-[(2-methoxy-5-methyl-4-sulfophenyl)azo]-2-naphthalenesulfonic acid, but also

known as “azo” dye. By itself Red 40 has an orangish-red color and found in cherry and strawberry flavored foods. Orange foods are typically dyed with Yellow 6. See Yellow 6. All dyes are considered additives by the FDA through the Federal Food, Drug, and Cosmetic Act (FD&C Act) since it is not used for the purpose of consumption, but to improve the appearance of the product. For example, chocolate pudding would be slightly greener without the use of red dye. Not just limited to foods, Red 40 is also used for coloring in cosmetics and sold as powders or liquids.

"Electronic Code of Federal Regulations." GPO Home Page. Title 21. Part 74, 12 May 2011. Web. 16 May 2011. .

FD&C Red Dye #40 Information, Education and Discussion. Web. 16 May 2011. .