there's an odd thing going on, I hope you can help me with this tricky issue :-)
Since milk contains a lot of potentially allergenc proteins, one must make a distinction:
Bovine serum albumin
Casein is heat stable, whereas the last three guys (the whey section) is heat labile.
Now that this is clear, we come to the actual problem:
A patient was prick-testet for (IgE-mediated) food allergies and showed a reaction to raw milk, but no reaction to casein itself and milk that has been cooked at 100?? for 10 minutes. This can only mean, that he's allergic to the whey section of the milk, since they are heat labile.
Now that the only possibility of a cross reaction to beef is the BSA (bovine serum albumin), which is not heat stable, he should be able to eat well cooked beef without any issues.
BUT: Eating well cooked ground beef resulted in severe diarrhea - and I have no clue why.
Are there any other connections between dairy an beef, except the BSA protein? And if no, why didn't cooking the beef remove the allergenicity of BSA?
Thanks in advance!
asked byThomy (2384)
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on December 29, 2011
at 05:44 PM
If this patient never consumed cooked ground beef before in their entire lifetime, the fat probably didn't agree with their GI tract. It makes no sense whatsoever to believe that the proteins in cooked beef would cause an allergic reaction or severe GI upset. HOWEVER, a quick check on google shows articles about WHEY protein being added to ground beef, something worth looking into? It depends on whether: this patient has eaten beef before and without gi upset, then there really is not a question to be answered right?
on December 17, 2019
at 06:26 AM
Few people with cow’s milk allergy may also develop allergy to beef. So, people having allergy to cow’s milk should avoid eating beef and foods containing beef.
on December 31, 2011
at 10:48 PM
I think I've found the solution (in case anybody has a similar issue):
BSA seems to be quite resistant to cooking and also to human digestion. So even cooked ground beef can trigger a reaction.
on December 15, 2019
at 07:32 PM
3. Bovine SA
BSA is one of the most well known proteins because of its widespread availability, similarity to HSA, use in medical formulations, and incorporation into many medical and biochemical assays. It is present in beef  and cow’s milk . BSA is used as a component of many vaccines [16,17], such as MMR, MMRV, Varicella, and Zoster, and is an important part of the culture medium used in artificial insemination. It is also studied because of its allergenicity; BSA has been identified as a minor allergen in bovine dander and serum .
Cow’s milk allergy is one of the most common food allergies, together with allergies to eggs, fish, and peanuts. In most cases childhood allergy to cow’s milk does not persist into adulthood; only 10–15% of young children diagnosed with the allergy remain so over five years of age [19,20]. A majority of patients with persistent milk allergy are also allergic to bovine serum albumin ; IgE from the affected patients was shown to be reactive toward several mammalian danders and meats. These patients have a greatly increased risk of developing rhinoconjunctivitis or asthma due to animal epithelia.
Very rarely, contact with BSA may cause an anaphylactic reaction. It was reported to be responsible for anaphylaxis in an artificial insemination patient . The patient was previously diagnosed with asthma and shown to have subclinical allergy to mammalian serum and thus cross-reactivity with BSA was suggested to be the origin of the anaphylactic reaction. Another patient with respiratory allergic reactions to feline epithelium had episodes of anaphylaxis after contact with BSA ; in this case the patient could tolerate well-cooked beef. More recently, it was reported that inhalation of BSA during work in a laboratory induced asthma in a patient .
The observation that thorough cooking of food improves tolerance is quite common in reports describing allergic reactions to SAs. Heat treatment has been shown to modify the allergenicity of beef and BSA and reduce, but not eliminate, their capacity to bind IgE from patients [21,25,26]. However, heat treatment in the presence of reducing agents was able to eliminate IgE binding, suggesting disulfide bridges were preserving the structure [26,27].
BSA is important in our understanding of SA allergenicity and the cross-reactivity of BSA with SAs from other animals has been studied extensively. The binding of IgG and IgA antibodies were studied by Hilger and coworkers , who found significantly higher anti-BSA titers in individuals suffering insulin-dependent diabetes mellitus. Furthermore, the N-terminal region of BSA degraded first in simulated gastrointestinal fluid. This agreed with the result that the IgG to IgA ratio was altered for this region because the epitope was destroyed before reaching the gut-associated lymphoid tissue. Other studies identified residues 524–598 of BSA as forming the IgE epitope , of which residues 524–542 were the most critical for antibody binding. Several previous studies also suggested that this fragment of the BSA sequence was immunogenic [18,30,31,32]. Fergusson et al. and Wahn et al. also showed that the N-terminal part of the protein is immunogenic, identifying residues 115–184 and 1–306 specifically. In addition, the so-called ABBOS epitope (residues 126–144) was suggested to be responsible for an autoimmune reaction against pancreatic islet cells, which leads to islet cell dysfunction . For a more detailed summary of epitopes relevant to bovine, horse and rabbit albumins see Majorek et al. (2012) as well as references therein.