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Health effectsEdit
The European Food Safety Authority (EFSA) reviewed the scientific
literature and published a review in 2009. As part of their evaluation,
the EFSA looked at the laboratory studies that have been done
on BCM-7. They found that experiments in cells and animals have
shown that BCM-7 can act as a weak opioid receptor agonist, but that
in most of the animal studies, BCM-7 was not administered orally, as
humans would be exposed to it, but rather was given to animals by
injection into the peritoneal cavity or even directly into the spinal cord
or brain, which makes these studies not useful for understanding how
BCM-7 might affect humans.[1] The EFSA found no relationship
between chronic diseases and drinking milk with the A1 protein.[1] The
EFSA study emphasized the dangers of drawing conclusions from
correlations identified in epidemiological studies and the dangers of
not reviewing all the evidence at hand.[1] Another 2009 review found
no demonstration that consuming milk with A1 casein causes
diabetes.[2] A 2014 review of research into the relationship between
consumption of dairy products (including A1 and A2 proteins) and the
incidence of diabetes found that while there appears to be a positive
correlation between consumption of dairy products by babies and the
incidence of type 1 diabetes (T1D) in some people, and an inverse
relationship between the consumption of dairy products and the
development of type 2 diabetes (T2D) in some people, these
correlations are tentative, it is impossible to determine what
component or components of milk might be responsible for these
effects, and it is unlikely that the expensive and complex research to
determine the answers to these questions will ever be conducted.[3]
A2 milk is not a milk substitute for infants with cow milk protein
allergies.[4]
The a2 Milk Company claims that people who experience discomfort
drinking ordinary cows' milk, may experience relief when they switch
to a2 Milk.[5][6][7]
HistoryEdit
In the 1980s, some medical researchers began to explore whether
some peptides (including peptides from casein) that are created
during digestion might have negative[8] or positive health effects.[1]
Interest in the distinction between A1 and A2 beta-casein proteins
began in the early 1990s via epidemiological research and animal
studies initially conducted by scientists in New Zealand, which found
correlations between the prevalence of milk with A1 beta-casein
proteins in some countries and the prevalence of various chronic
diseases in those countries.[9] The research generated interest in the
media, among some in the scientific community, and entrepreneurs.
[9] If it is indeed true that BCM-7 is harming humans, this would be an
important public health issue, as well as a commercial opportunity.[9]
Cows' milk is about 87 percent water and 13 percent solidsthe
solids being a combination of fat, carbohydrates in the form of
lactose, minerals and protein. The major component of the milk
proteins is casein; in turn about 30-35 percent of the casein
(equivalent to two teaspoons in a litre of milk) is beta-casein, of which
there are several varieties, determined by the genes of the cow. The
most common of these variants are A1 and A2 (named for the order in
which they were identified by scientists), with the sole difference
between the two being one of the 209 amino acids that make up the
beta-casein proteins: a proline occurs at position 67 in the chain of
amino acids that make up the A2 beta-casein, while in A1 beta-casein
a histidine occurs at that position. Studies in cells found that digestive
enzymes that cut up proteins interact with beta-casein precisely at
that location, so that A1 and A2 beta-casein proteins are processed
differently. A seven-amino peptide, beta-casomorphin-7, (BCM-7) can
be cut away from the A1-beta-casein protein by those enzymes, but
the enzymes cannot cut the A2 protein at that location, so BCM-7 is
not formed from A2 proteins.[9] Studies in humans have not
consistently found that BCM-7 is formed in the human digestive
system.[2] BCM-7 can also be created during the fermentation of milk
or through the process by which cheese is made; those same
processes can also destroy BCM-7.[1]
Scientists believe the difference originated as a mutation that
occurred between 5000 and 10,000 years agoas cattle were being
taken north into Europewhen the proline at position 67 was replaced
by histidine, with the mutation subsequently spreading widely
throughout herds in the western world through breeding.[9][10]
The percentage of the A1 and A2 beta-casein protein varies between
herds of cattle, and also between countries and provinces. While
African and Asian cattle continue to produce only A2 beta-casein, the
A1 version of the protein is common among cattle in the western
world.[9] The A1 beta-casein type is the most common type found in
cow's milk in Europe (excluding France), the USA, Australia and New
Zealand.[1]:20 On average, more than 70 percent of Guernsey cows
produce A2 milk, while among Holsteins and Ayrshires between 46
and 70 percent produce A1 milk.[11]
A2 CorporationEdit
Main article: the a2 Milk Company
A company, A2 Corporation, was founded in New Zealand in 2000 to
commercialise a genetic test to determine whether a cow will produce
milk without the A1 protein, and to market "A2 Milk".[9][12][13] In 2003,
A2's website said: "Beta casein A1 may be a primary risk factor for
heart disease in adult men, and also be involved in the progression of
insulin-dependent diabetes in children" and the CEO had linked A1 to
schizophrenia and autism.[14] A2 Corporation also petitioned the Food
Standards Australia New Zealand regulatory authority to require a
health warning on ordinary milk.[9]
A2 Corporation was succeeded by The a2 Milk Company.
A2 milk
La leche A2 es leche de vaca que contiene slo el tipo A2 de protena beta-casena
en lugar de la protena A1 ms comnmente encontrada en la leche regular. La
leche A2 es licenciada y comercializada por la a2 Milk Company y vendida
principalmente en Australia, Nueva Zelanda, China, Estados Unidos y el Reino
Unido.
HistoriaEditar
En los aos ochenta, algunos investigadores mdicos comenzaron a explorar si
algunos pptidos (incluyendo pptidos de casena) que se crean durante la
digestin podran tener efectos negativos [8] o negativos para la salud.
El inters en la distincin entre las protenas A1 y A2 beta-casena se inici a
principios de los aos 90 a travs de la investigacin epidemiolgica y los estudios
en animales realizados inicialmente por cientficos en Nueva Zelanda, que encontr
correlaciones entre la prevalencia de la leche con A1 beta-casena protenas en
algunos pases y la Prevalencia de varias enfermedades crnicas en esos pases. [9]
La investigacin gener inters en los medios de comunicacin, entre algunos de la
comunidad cientfica, y los empresarios. [9] Si realmente es cierto que BCM-7 est
daando a los seres humanos, esto sera un importante problema de salud pblica,
as como una oportunidad comercial.
La leche de las vacas es de aproximadamente el 87 por ciento de agua y el 13 por
ciento de slidos. Los slidos son una combinacin de grasa, carbohidratos en
forma de lactosa, minerales y protenas. El componente principal de las protenas
de la leche es la casena; A su vez alrededor del 30-35 por ciento de la casena
(equivalente a dos cucharaditas en un litro de leche) es la beta-casena, de la cual
hay varias variedades, determinadas por los genes de la vaca. El ms comn de
estas variantes son A1 y A2 (nombrado para el orden en que fueron identificados
por los cientficos), con la nica diferencia entre los dos que es uno de los 209
aminocidos que componen las protenas de la beta-casena: una prolina ocurre En
la posicin 67 en la cadena de aminocidos que forman la beta-casena A2,
mientras que en la beta-casena A1 se produce una histidina en esa posicin. Los
estudios en clulas encontraron que las enzimas digestivas que cortan las protenas
interactan con la beta-casena precisamente en esa ubicacin, de modo que las
protenas A1 y A2 beta-casena se procesan de manera diferente. Un 7-amino
pptido, beta-casomorphin-7, (BCM-7) puede ser cortado de la protena A1-beta-
casena por esas enzimas, pero las enzimas no pueden cortar la protena A2 en ese
lugar, por lo que BCM-7 es No formado a partir de protenas A2. [9] Los estudios en
seres humanos no han encontrado consistentemente que BCM-7 se forma en el
sistema digestivo humano. [2] BCM-7 tambin se puede crear durante la
fermentacin de la leche o mediante el proceso por el cual se hace el queso; Esos
mismos procesos tambin pueden destruir BCM-7. [1]
Los cientficos creen que la diferencia se origin como una mutacin que ocurri
entre 5000 y 10.000 aos atrs -como el ganado se estaba llevando al norte a
Europa- cuando la prolina en la posicin 67 fue reemplazada por la
histidina, con la mutacin extendindose posteriormente a travs de los rebaos
en el mundo occidental a travs de Cra. [9] [10]
A2
Corporacin Editar seccin
Artculo principal: la Compaa de Leche a2
Una empresa, A2 Corporation, fue fundada en Nueva Zelanda en 2000 para
comercializar una prueba gentica para determinar si una vaca producir leche sin
la protena A1, y comercializar "A2 Leche" [9] [12] [13] En 2003, la pgina web de
A2 dijo: "La beta casena A1 puede ser un factor de riesgo primario para la
enfermedad cardaca en hombres adultos, y tambin participar en la progresin de
la diabetes dependiente de la insulina en los nios" y el CEO haba vinculado A1 a
esquizofrenia y autismo. [14] A2 Corporation tambin solicit a la autoridad
reguladora de los Estndares Alimentarios Australia Nueva Zelandia que requiriera
una advertencia de salud en la leche normal. [9]