Miscellaneous references:C:\netscape\html\miscref.txt
01]Herring PT, Irvine JC, MacLeod JJR, The Efficiency of Various Sugars
and their Derivatives in Relieving the Symptoms Caused by Insulin in Mice,
Biochemical Journal, Volume 18, Article 135, 1023-1042,1924.
02]p. 1025: glucose effects permanent cure of insulin overdose in non-
diabetic rabbit. But Nobel and Macleod that fructose and galactose
do not effect permanent cure, relapses occur after temporary improve-
ment.
03]Their method was to give a lethal dose of insulin, and to test for
complete recovery by various sugars.
04]Mannose (5 minims) brought about complete recovery in 4 minutes which
was permanent.
05]Maltose effected complete recovery in 15 of 16 mice, but in slower order
than glucose or mannose, and requires higher doses. In rabbits, Noble and
Macleod found maltose similar to fructose and galactose.
06]Lactose had no effect. Same with rabbits.
07]Sucrose is incapable of alleviating symptoms of hyper-insulination in mice
or rabbits.
08][Neither alpha or beta methylglucoside showed slightest activity, nor tetra-
methyl-B-methylglucoside; tetra-gamma-"-".
09]Glucose monoacetone is inactive.
10]Salicin seemed to cause harm, with hemorrhage to the lungs of one mouse.
But did seem to have some activity in a few mice. Difficult to interpret.
Thus considered toxic.
11]The alcohols related to the sugars were tested:
Mannitol is inactive.
Dulcitol is inactive.
12]The anhydro-sugar Beta-glucosan is inactive.
13]asymmetry and a reducing group must be present to cure. Glucose, mannose
and in a slower action, amylose satisfy these.
14]Macleod found maltose in rabbits was decidedly more effective than fructose
or galactose.
15]Bial (1893) and Hamburger (1895) demonstrated maltase in the blood, and
this doubtlessly accounts for maltose effect.
get:]Bial, 1893, Pfluger's Arch. 53, 156; 54, 72.
get:]Hamburger, 1895, Pfluger's Arch. 60, 543.
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Same Journal:
Article 134, page 1009
16]The Catalytic Action of Traces of Iron on the Oxidation of Cysteine and
Glutathione, By D.C.Harrison.
Summary:
1. The purification of cysteine and glutathione has been carried out using
quartz vessels and taking special precautions to remove iron. Much of the
work of Warburg and Sakuma on cysteine have been confirmed.
2. The rates of atmospheric oxidation of both cysteine and glut. are found
to be very greatly reduced by the removal of traces of iron impurities.
3. It has been shown that the addition of quantities of iron of the order
of 1/10,000 mg. produces a marked increase on the rate of oxidation of the
purified cyst. and glut.
4. Evidence has been given that the inhibition in the oxidation of cysteine
and glutathione by hydrogen cyanide is due to its forming a complex with the
catalytic iron.
5. The velocities of oxygen uptake in the case of the purified compounds
alone, and in the case of the unpurified compounds in the presence of
cyanide, have been found to be linear.
6. It has been found that the iron in haematin is also capable of catalysing
these oxidations.
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17]World Review of Nutrition and Dietetics, 11:106-141, 1969.
M. Narayana Rao and M. Swaminathan, Plant Proteins in the Amelioration of
Protein Deficiency States
Sections I-IX
Sec. V, B. Toxic Factors:
Trypsin Inhibitors: A trypsin inhibitor from soya beans was first isolated
by Kunitz [1945]. this was a protein, having a molecular weight of about
20,000 and forming an inactive complex with trypsin. Active antitrypsin
fractions from raw soya beans retard growth of rats, mice and chicks
[BORCHERS, ACKERSON, MUSSEHL and EOCHL, 1948]. There is still a decided
lack of agreement as to the mechanism by which the tryptic inhibitor exerts
a growth-inhibiting effect. Feeding of soya beans causes pancreatic hyper-
trophy, which leads to an excessive loss of endogenous protein in the form
of exocrine protein, secreted by the pancreas [CHERNICK, LEPKOVSKY and
CHAIKOFF, 1948; BOOTH, ROBBINS, RIBELIN and DE EDS, 1960]. This protein
is rich in cystine and the increased need for cystine for protein biosyn-
thesis during pancreatic hypertrophy is reflected by an increase in the
conversion of methionine to cystine in the pancreas [BARNES and KWONG, 1965].
This explains partly the need for methionine in counteracting the
deleterious effect of raw soya bean diets. RACKIS and ANDERSON [1964]
showed the presence of four trypsin inhibitors, each of which produce dif-
ferent physiological effects.
The presence of trypsin inhibitors in peanuts, navy beans, lima beans and
kidney beans has also been reported [HAM and SANDSTEDT, 1944; KLOSE, HILL,
GREAVES and FEVOLD, 1949]. PUSZTAI [1967] has summarized the present status
of trypsin inhibitors of plant origin, their chemistry and potential role
in animal nutrition.
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TABLE VIII. Tonic factors present in vegetable protein foods.
------------------------------------------------------------
Protein food Botanical name Toxic factors
------------------------------------------------------------
Legumes
Red gram Cajanus cajan Tryptic inhibitor
Chick-pea Cicer arietinum " "
cyanogenetic glycosides
Green Gram Phaseolus aureus Tryptic inhibitor
Hemagglutinin
Lentil Lens esculenta Tryptic inhibitor
Hemagglutinin
Cow-pea Vigna catiang Tryptic inhibitor
Khesari dhal Lathyrus sativus Beta-N-oxalyl-alpha,
Beta-diamino-proprianic acid
Peas Pisum sativum Hemagglutinin
Goitrogenic factor
Oil seeds
Peanut Arachis bypogea Goitrogenic factor
Trypsin inhibitor
Hemagglutinin
Soya bean Glycine max Tryptic inhibitor
Hemagglutinin
Goitrogenic factor
Saponins
Toxic histone-like protein
Anticoagulant
Cotton seed Gossypeum herbaceum Gossypol
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LIENER, [1966] discusses toxic factors in vegetable protein, including
saponins, histones, metal binding factors, antivitamin factors,
cyanogens, etc. Also how heat destroys most of these factors [1958].
Fermentation increases protein availability of soya, but data as to the
effect on trypsin inhibitors is not discussed, but see [CHENG, KE and YOON,
1959; GRORGY, 1961; CHOELHO and BHAT, 1959]. Fermented products: Tempeh
and Natto.
get references from bibliography:
get:]RACKIS JJ, AND ANDERSON RL: Isolation of four soyabean trypsin
inhibitors by DEAE-cellulose chromatography. Biochem. biophys. Res.
Commun.15:230-235, 1964.
get:]LIENER IE: Soyin, a toxic protein from the soyabean. I. Inhibition of
rat growth. J. Nutr. 49:527-539, 1953.
get:]LIENER IE: Effect of Heat on plant proteins. In "Processed Plant
Protein Foodstuffs", ed. A.M. Altschul, pp. 79-129 (Academic Press,
1958)
get:]LIENER IE: Toxic substances associated with seed proteins. In 'World
Protein Resources', ed. R.F.GOULD, pp. 178-194 (American Chemical
Society,Washington, 1966).
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18]See C:\netscape\html\ocr\laetrile\Narayan01-?.txt
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19]This note scribbled on scratch card: Liquor potassae dissolves benign
tumors. No idea what the source was, doesn't appear to be in Eli P. Jones'
work, nor Parke-Davis Manual of Therapeutics. Check out.
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Karger: http://www.Karger.ch
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Rob van Hattum: Postbus 1, 1200 JC Hilversum, Tel: (035)6712911.
Producer of a film on Rife.
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20]For laetrile, the Encyclopedia Brittanica 1937 notes that amygdalin can
be activated by maltase. In Somer and Sumner, Chemistry and Methods of
Enzymes, 1943, p. 72, notes that Maltase was discovered by Musculus, and
Gruber. That maltase is also called alpha-glucosidase. Maltose and sucrase
are alpha-glucosides. Alpha-glucosidase was suggested by Weidenhagen to be
identical with animal sucrase, but this was questioned by Myrback..
21]But see item [15] Bial and Hamburger, so possible sequalae of nitriloside
parenterally.
22]Silver, cupric and mercuric ions inactivate beta-glucosidase. Oxidizing
agents cause inactivation. p.74.
23]It apparently attacks a few alpha-glucosides.
24]rsc: Considering that the cancer glyco-protein is 34% carbohydrate,
consisting of:
[see C:\europa11\eudora2\trophref.txt, item [8] and ff.]:
=======================================
hCG Carbohydrate composition (Om.P.Bahl, in: Gonadotropins: Studies on the
Primary Structure of hCG and its Relationship to other Glycoprotein
Hormones)
(residues 28,000 molecular) [according to table II, p. 202]
L-fucose (1)
D-mannose (9)
D-galactose (9)
Glucosamine (11)
Galactosamine (3)
sialic acid (8)
2-acetamido-2-deoxy-D-glucose & 2-acetomido-2-deoxy-D-galactose (?)
On p. 200, he listed fucose, galactose, mannose, and the above acetamindo-
forms, as well as the rotations in the table quoted. Not sure if these form
galactosamine or glucosamine.
++++++++++++++++++++++++++++++++++++++++++
24 cont] then almonds which contain beta-galactosidase (Somer and Sumner,
1943, p. 75, 76; and beta-glucuronidase, pg. 77, in almonds? but says so,
although this is elsewhere termed as a liver and spleen enzyme), might
actually help in the degradation of the hormone hCG, as well as the
membrane-bound glycoprotein.
25]rsc: determine the actual per cent content of apricot kernel for
all enzymes, fats, sugar, total carbohydrate, and total protein.
26] Somer and Sumner's work is weak on carohydrases, but good refs.:
get:] Marker M: Chem. Centralblatt 1878, 559. Says malt-amylase is two
enzymes.
27] They state that amylase is found:
a) especially in sprouted seeds. p. 81
b) Amylases are found in blood plasma and
c) leucocytes (source not given for these datums unless its:
get:] COHN, EW, and BROOKES MH, J. Biol. Chem., 115, 139, 1937.
get:] SUMNER JB, AND HOWELL SF: J. Biol. Chem., 108, 51, 1935.
get:] STAMBERG OE, AND BAILEY CH:J. Biol. Chem., 126, 479, 1938.
get:] TELLER GL: J. Biol. Chem. 115, 425, 1936(?)
get:] FORD JS, AND GUTHRIE JM: J. Inst. Brew. 14, 61 (1908).
28] Ford and Guthrie observed bound amylase can be activated by papain.
(quoted in Sumner and Somers, p. 82.) Sumner and Somers also noted that
Chrzaszcz (pronounced "Shonts") and Janicki used eluants, trypsin,
chymosin, and hydrogen sulfide to also activate bound amylase.
29] Waldschmidt-Leitz and Mayer found an enzyme that liquifies starch jelly
but which did not result in sugar. p. 82. "..amylo-phosphatase".
rsc: Could be used in cancer without throwing blood sugar off?
Quote:
"Kidney phosphatase has the same action. According to Mayer and Klinga-Mayer
(51) the three enzymes in barley which act upon starch are amylase, amylo-
phosphatase and pyro-phosphatase." p. 82.