This is why pork has a lot of thiamin in it.. it has to make for the inefficient thaimine triphosphatase .. so I'm still unsure if that means that pork thiamin isnt as efficient when eaten by humans or not!!!

Pork is said to contain very high thiamin levels ..and I confirm it after eating Xmas osk and observing my son's preference for sweet and sour pork in Chinese cooking and how I feel better if I eat at least some of the pork too with the white rice.
I used to wonder why I'd feel wiped otherwise..now I know what to do to avoid being wiped after Chinese.. it wasnt the MSG after all.. the restauarnt owner/cook always claimed he used none..and he was a friend of my daughters who worked there too for a while.

Edited -added end Jan2007
Over Xmas and for a few weeks after I ate a LOT of ham (having bought half a leg of ham and frozen some of it in pieces).
I found I started too easily gaining weight and needed steadily reducing amounts of B1 .. just packing on the tummy ..like premenopausal weight gain(only it didnt stop, I used to go from a non US 9 to a 13 premenopausally and lose it with periods..)..and had to stop the injections altogether. I found after a while I started gradually (very slowly) losing the weight and becoming ,more fatigued and constipated as the ham in my body decreased (after i stopped eating it for a few days).

I had to start injecting B1 again.
I also noted the hit after having Armour when not eating the ham or taking B1.. so started on b1 again (of course not to the same extent as b4 now I know what causes the extreme fatigue hit of taking Armour.. it maybe depletes the B1?).
Would pig's thryoid consume more B1 than our thyroids.. pigs storing way more b1 in their tissues..?? Is there something in this??

Then I defrosted my last piece of pork and continued with the injections, as i steadily build up my B1 levels again and fatiigue goes away.
i also needed almost double the amount of T4 and thryoid (pig's thryoid) when i didnt take the ham or B1 injections..
since going back to both I've noticed the fatigue go away agian and I can lessen my b1..
so its got something to do with this ham having more B1

also Armour (my thryoid IS pig's thryoid.. maybe that somehow uses up more B1 than T4 (synthetic) or even cows thryoid does?.. just a thought.. havent really thougt this thru.. but the ham definitely means I dont need the B1 injections
similarly I always felt better if I ate sweet and pur pork in Chinese restaurant..I always felt bad if I consumed the rice (which is white with NO added thiamin as in the US and Canada).. and didnt have the sweet and sour pork..
also my eldest son John always orders only this pork too in Chinese..
and he too ahad a lot of urine as a baby on cows milk.. drank upwards of 12 bottles a day.. and opeeded almost constant bith large amounts and frequently..
couldnt reduce this amount.. he cried (screamed) until he got it..and he couldn't wait either(I really think he couldn't.. he was extremely distressed)..the reason I first purchased a microwave.. to heat the bottles
I bet its all linked together somehow with this B1 stuff?

just jotting down some thoughts here----------------------------

: Biochim Biophys Acta. 2005 Aug 30;1725(1):93-102. Links
Pig tissues express a catalytically inefficient 25-kDa thiamine triphosphatase: insight in the catalytic mechanisms of this enzyme.Szyniarowski P, Lakaye B, Czerniecki J, Makarchikov AF, Wins P, Margineanu I, Coumans B, Grisar T, Bettendorff L.
Center for Cellular and Molecular Neurobiology, University of Liege, B-4000 Liege, Belgium.

Thiamine triphosphate (ThTP) is found in most organisms and may be an intracellular signal molecule produced in response to stress. We have recently cloned the cDNA coding for a highly specific mammalian 25-kDa thiamine triphosphatase. The enzyme was active in all mammalian species studied except pig, although the corresponding mRNA was present. In order to determine whether the very low ThTPase activity in pig tissues is due to the absence of the protein or to a lack of catalytic efficiency, we expressed human and pig ThTPase in E. coli as GST fusion proteins. The purified recombinant pig GST-ThTPase was found to be 2-3 orders of magnitude less active than human GST-ThTPase. Using site-directed mutagenesis, we show that, in particular, the change of Glu85 to lysine is responsible for decreased solubility and catalytic activity of the pig enzyme. Immunohistochemical studies revealed a distribution of the protein in pig brain very similar to the one reported in rodent brain. Thus, our results suggest that a 25-kDa protein homologous to hThTPase but practically devoid of enzyme activity is expressed in pig tissues. This raises the possibility that this protein may play a physiological role other than ThTP hydrolysis.

PMID: 16000236 [PubMed - indexed for MEDLINE]