Ta k e u c h i (Sei-i-kwai Med. J., 1930, 4 9 , No. 9, 74—
87).—Quant, changes in blood- and urinary N ex
hibited by rabbits on subcutaneous injection of thebaine, dihydrothebaine, oxycodcinone, and di- hydrohydroxycodeinone hydrochlorides are recorded.
Chem ical Abst r a c ts,
Effect of India ink and of tolylenediam ine on the augm enting properties of bile salts on glyco
gen synthesis by the liver. S. Fu jit a (Arb. Med.
Univ. Okayama, 1931, 2 , 557—565).—Small amounts of C7H6(NH2)2 are slightly synergistic, but larger amounts, or India ink, are antagonistic, to the augmenting influence of bile salts on the glycogen- synthesising property of the liver.
Chem ical Abst r a c ts.
Pharm acological actions of som e alkyl deriv
atives of harm ol. II. Propylharm ol. G. K.
El p h ic k and J. A. Gu n n. III. Butylharm ol.
J. A. Gu n n and M‘. H. MacKe it h. TV. A m yl- harm ol. V. Nonylharm ol. G. K. El ph ic k and J. A . Gu n n (Quart. J. Pharm., 1932, 5 , '37—47, 48—55, 56—62, 63—71).—With increasing length of side-chain, general symptoms in the frog appear more slowly; increased motor excitability in mammals is decreased, with correspondingly earlier onset of paralysis; contracture of voluntary muscle occurs less readily; stimulation of uterus decreases and inhibition "becomes more marked. In small doses, all except the Bu compound cause pressor effects, and in larger doses all produce a fall in blood-pressure.
Respiration is depressed in the order Pr>Et, whilst Bu, amyl, and nonyl compounds always cause acceler
ation, nonyl being much slower in action than the
6 4 8 B R IT IS H C H E M IC A L A B S T R A C T S .— A .
others. Mammalian coronaries are dilated and heart-muscle is depressed in the order amyl^>Pr > Et>
Bu^>nonyl. The isolated intestine is relaxed by moderate doses of amyl, Bu, Pr, Et (Pr>Et) and stimulated by minute doses. Nonylharmol is by far the most toxic to protozoa and slowest in action.
J. B . Ba t e m a n.
Pharm acological action of new choline deriv
atives in relation to their chem ical constitution.
W. F. v o n Oe tt in g e nand D . F. Ev e l eth (J. Pharm.
Exp. Thor., 1932, 44, 465—477).—Substitution of the alcoholic OH group by Cl or the quaternary trimethylammonium chloride radical reinforces the characteristic choline actions, whereas substitution by NH2- and NHMe-groups increases the depressant action on muscular tissue; hence it follows that the
•NMe3-C2H4‘ nucleus is pharmacologically the essential part of the choline molecule. H. Dav so n.
Neutralisation of toxic properties of strychnine sulphate. A. C. Mar ie (Ann. Inst. Pasteur, 1932, 48, 449—456).—IvMn04 will neutralise the toxicity of about an equal wt. of strychnine sulphate. Neither adrenaline nor blood alone shows any effect, but together they detoxicate strychnine sulphate; the blood may be replaced by bile. The alkaloid is non-toxic even when extracted from the mixture by Et20, but regains its toxicity on reduction by Na2S204. The effect is due to a preferential oxidation of strychnine in presence of adrenaline.
P. G. Ma r sh a l l.
Sperm icidal activity of quiñones and quinols.
J. M. Gu l l a n d (Biochem. J., 1932, 2 6 , 32—45).—
The toxicities to spermatozoa of many phenols, quinols, and o- and p-quinones have been determined.
The greater toxicity of p-quinones and quinols is related to their greater chemical reactivity. Intro
duction of an alkyl group into p-benzoquinone enhances activity, but further alkylation decreases the toxicity. Aromatic o-hydroxyaldehydes are more spermicidal than the m- or p-derivatives. The following are new : 2 : 5 -d ih y d r o x y p lic n y l P r ketone,
m. p. 87—-89°; 2 : 5 -d ih y d ro x y b u ty lb e n ze n e , m. p.
89°; b u t y l - l : i-b e n z o q u in o n e , m. p. 32°. A. Co h e n.
Calcium therapy. M. Bú f a n o (Clin, méd., 1928, No. 6; Rev. sud-amer. endocrinol., 1931, 14, 705—
706).—After intramuscular injection of CaCl2 (0-15 g.) the blood-Ca is increased for 24 hr.; the increase in K is slower. The use of Ca gluconate does not always cause higher calcsemia; the ratio K : Ca is always low.
Chem ical Ab st r a c t s.
Form ation of w heals. IV. Influences of calc
ium concentration on histam ine w heals. W. K.
We a v e r, H. L. Al e x a n d e r, and F. S. McCo n n e l l
(J. Clin. Invest., 1932, 1 1 , 195—209).—Ingestion of NH,C1 decreases, and of NaHC03 increases, histamine wheals; an explanation involves change in Ca concn.
Chem ical Abst r a c ts.
Cadm ium poisoning. I. H istory of cadm ium poisoning and u ses of cadm ium . L. Pro dam (J.
Ind. Hygiene, 1932, 14, 132—155).
Effect of phosphate and hydrogen carbonate buffers on ionisation of calcium salts in physio
logical salt solutions. W. F. v o n Oe t t in g e n and R. E. Pick ett (J. Pharm. Exp. Ther., 1932, 44,
435—443).—Ca ions are determined by measuring their effect on a drop of castor oil floating on H20 in presence of soap. Concns. of the order of 0-03%
of NaHCOj and 0-008—0-048% phosphate buffers cause association of the Ca ions. The effect of phosphate buffers is modified by the addition of 0-008—0-015% of NaHC03. H. Davson.
Influence of light-rays on the total cholesterol content of the skin. S. Ka w a g u c h i (J. Biochem.
Japan, 1932, 1 5 , 111—114).—Artificial irradiation of the rabbit results in an increase of cholesterol and its esters in the skin. The H20 content is also
increased. F. O. flowin'.
Synthesising action of enzym es. R. Ammon
(Angew. Chem., 1932, 4 5 , 357-—359).—A review.
Laws of com bination of enzym es w ith sub
strates. H. Fisch go ld and R. Amm on (Biochem.
Z., 1932, 2 4 7 , 338—353).—All enzymic processes which can be explained on the basis of the law of mass action (Michaelis and Menten) can also be based on Langmuir’s adsorption theory. The lack of conformity to the theories at high substrate concns.
is a consequence of elimination of H20 from the surface of reaction. The reversal of the direction of optical rotation produced by some esterases when the concn. of the substrate is high may be due,
if the adsorption theory is assumed, to differing sensitivity of the two diastereoisomeric enzyme- substrate compounds, to the decreased concn. of Il20 in the region of reaction, or to alteration in the proportions of the two antipodes resulting from change in the concn. of the substrate. A third possibility is that the enzyme undergoes irreversible alteration when this concn. becomes high.
W . McCartney.
Determ ination of oxidase. T. Hana za w a(Trans.
Tottori Soc. Agric. Sci., 1931, 3, 187— 194).—The neck of the flask containing the sample is provided with side-tubes and containers for Ar-NaOH (25 c.c.) and 1% pyrocatechol solution (10 c.c.) and with a mineral-oil manometer. The O, absorption for 100 c.c. of potato juice was about 40 mg.
Chem ical Abstracts.
M ilk-peroxidase. Preparation, properties, and action w ith hydrogen peroxide on meta
bolites. D eterm ination of sm a ll amounts of hydrogen peroxide in com plex m ixtures. K. A. C.
Elliott (Biochem. J., 1932, 2 6 , 10—24).—A crude conc. peroxidase free from catalase is obtained from milk by fractional pptn. with (NH4)2S04. The prep, loses activity very slowly at 0—5°, and is active between pH 4 and 10. Thiol compounds interfere with peroxidase tests using benzidine, guaiacum, and p-phenylenediamine. H20 2 is determined by measuring the 0 2 liberated by Mn02. Under con
ditions suitable for the complete oxidation of NaN02 by H202 in the presence of peroxidase, no oxidation of formate, acetate, oleate, stearate, triolein, EtOII, glucose, glycerol, MeCHO, ¡3-hydroxybutyrate, lactate, glycine, phenylalanine, or histidine was o b s e r v e d ,
whilst tyrosine and tryptophan were oxidised to coloured products. Dihydroxyacetone and phenyl- glyoxal were oxidised by dil. H„0„ w-ithout peroxidase.
. “ " A. Cohen.
B IO C H E M I S T R Y . 6 4 9
Accelerating action of uric acid on the xanthine- oxidase system. D. C. Ha r r iso n (Biochem. J., 1932, 26, 472—475).—The inhibiting action of uric acid on the oxidation of hypoxanthine in presence of xanthine-oxidase and methylene-blue may be converted into an acceleration either by increasing the hypoxanthine or decreasing the enzyme concn.
The accelerating effect appears to be due to the replacement on the enzyme surface of the inhibitor hypoxanthine by the less powerful inhibitor uric
acid. S. S. Zil v a.
Tyrosinase and pseudo-peroxidase. S. Be r e n-
stein (Arch. Sci. phys. nat., 1932, [v], 14, 24—54).—
The various types of oxidising enzymes are discussed and classified. Pseudo-peroxidase, a dehydrogenase, occurs in C y p e r u s escu len lu s, L., and other plants, but is isolated from these sources only with difficulty.
Sweet almonds, however, readily yield the enzyme on aq. extraction. The extract is pptd. by EtOII, yielding an active ppt. In presence of NaHC03 and H202 the enzyme forms a red pigment from p-crcsol.
The additional presence of an NH2-acid, indole, or phloroglucinol results in the formation of character
istic pigments. The pigment yielded by an NH2- acid is identical with that produced by tyrosinase in presence of the NH2-acid; the presence of II20 2 is essential for pseudo-peroxidase to react in this way.
The accelerating influence of H20 2 on the p-cresol- tyrosinase reaction is not confirmed (cf. A., 1930, 1474). “ Cresol-azure,” the blue pigment from p -
cresol, is prepared by the action of potato-oxidase in presence of glycine; it is identical with the product from 3 : 4-toluquinone (A., 1911, i, 728) and glycine.
Solutions of this pigment show absorption bands at 530—610, 588, and 555 mg. The pigments from phloroglucinol (“ cresol-rubin ” ) and indole (“ indo- cresol ■” ) are similarly synthesised and examined.
F . 0 . How itt.
a- and (3-Amylase in malt and barley. E.
Waldsciim idt-Le itz, M. Reic h e l, and A. Purr (Naturwiss., 1932, 20, 254).—Treatment of a green- malt extract at p n 3-8 with A1203 gives in the mother- liquor the pure a-component, whilst in the alkaline washings of the adsórbate the (1 is found. In this method they may be separated from the natural activator of amylase, a m y l o k im s e . Barley contains both a- and [3-amylase, the a being in its inactive form; a-amylase seems necessary for the rapid con
version of starch into sugars. H. Da v so n. A c t io n o f c e l l u l a s e a n d h e m i c e l l u l a s e o n p la n t m a te r ia ls in vitro. K. S i lb e r s c h m id t (Miinch.
med. Woch., 1931, 78, 1819—1824; Chem. Zentr., 1931, ii, 3499).—Loss of sensitivity to cellulose dyes is followed by loss of sensitivity to pectin dyes, the effects being parallel with the softening of the cell membrane. A. A. E l d r i d g e .
Dilatometric investigation of enzymic pro
cesses. II. Di- and tri-saccharides. P. Ro n a, N. Ne u e n sc h w a n d e r-Lem m er, and H. Fisciigold
(Biochem. Z., 1932, 247, 257—274; cf. A., 1931, 983).—During the hydrolysis of lactose, cellobiose, end raffinose with enzymes (emulsin, invertase) and with dil. H2S04, vol. decreases proportional to the changes in optical rotation and similar to those
x x *
previously found with sucrose and maltose are ob
served. When more cone. acids are employed with cellobiose and lactose the decreases in vol. differ from those found with enzymes and dil. acids, whilst with maltose and glucose there is a vol. increase irregular for the former, regular for the latter. The mutarota- tions of glucose, galactose, and fructose are accom
panied by vol. changes related to the changes of form which occur during the process. In the case of glucose and galactose the vol. changes which accom
pany the complete change of one modification into the other are equal. W. McCa r t n e y.
Action of the alkaloids and carbon monoxide on the enzymic activity of plants. M. Pado a (Nature, 1932, 129, 686).—The addition of small amounts of strychnine nitrate increases the amylase activity of barley during germination, and the activities of lipase, amylase, protease, and oxidase in castor-oil seeds germinating in H20, but not the enzymic extracts of seeds. R ic in u s seedlings are improved by additions of strychnine nitrate and caffeine, but the latter is toxic towards barley, flax;
and other plants. Small amounts of CO stop the assimilatory activity of green plants in light but not the respiration; CO slightly increases the lipase activity but decreases the amylase activity of barley and of R ic in u s . Wheat, lupins, and peas germinate in an atm. rich in CO, cabbage and hemp germinate with difficulty, whilst flax and tomato fail. N assimilation in leguminous plants appears to be due, but not exclusively, to the stimulating action of N bacteria; it is also related to enzymic activities latent in the plants. L. S. Th e o b a l d.
Directive influences in biological systems. I.
Specificities of lipase actions. Iv. G. Falic
(J. Biol. Chem., 1932, 96, 53—71).—Tho action of pancreatic lipase on various simple esters alone and in presence of inactive proteins or of lipolytically active normal tissue- and tumour-extracts was in
vestigated. In addition to the protective action by tho added material there occurred interaction which resulted in selectively increasing certain of the hydro
lyses. It is suggested that lipase or ester-hydrolys
ing actions are due to a definite grouping on the en
zyme and that the sp. action of the added tissue extracts or proteins is due to certain characteristics of the added substance. F . O. Ho w itt.
Isolation of asparagine from an enzymic digest of edestin. M. Da m o d a r a n (Biochem. J., 1932, 26, 235—247).—Edestin was digested by the successive action of pepsin, trypsin, and yeast - dipeptidase with only slight splitting of amide-N, and asparagine was isolated from the digest. The presence of glutamine was also indicated by the method of Chibnall and Westall (cf. this vol., 660). A. Co h e n.
Proteolytic enzymes of the pancreas and intestine. (Ml l e.) E. Le Br e t o n (Bull. Soc. Chim.
biol., 1932,14, 417—506).—A lecture.
Proteolytic degradation of crystalline urease.
E. Waldsch m idt-Leitz and F. St e ig e r w a l d t (Z.
physiol. Chem., 1932, 206, 133—136).—It is re
affirmed that by the action of proteinase up to 80%
of the substance in cryst. urease precipitable by
65 0 B R IT IS H C H E M IC A L A B S T R A C T S .— A .
sulphosalicylic acid is destroyed without affecting the urease activity (cf. Sumner and Kirk, this vol., 544). J. H. Bi r k i n s h a w.
Crystalline urease. Preparation of meal from jack-beans. J. S. Ki r k and J. B. Su m n e r (Ind.
Eng. Chem., 1932, 24, 454—455).—A special grinder is described. P. G. Ma r s h a l l.
Uricase and its action. V. Ox-kidney uri- case. R. Tr u s z k o w s k i (Biochem. J., 1932, 26, 285—291).—Ox-kidney uricase suspensions do not yield fractions of different activity on sedimentation.
Both medullary and cortical tissues are active, the action of the latter being, however, about 25%
greater than that of the former. Uricase is irrever
sibly inactivated in solutions of p n 2—6-56, but not of p u 7-59, by neutral solutions of KCN, I (0-01—- 0-1N ) , H,02, FeS04, and HgCl2, but not by CuS04.
The enzyme is completely inactivated by heating for 5 min. ahove 70° and almost completely at 70°, partly at 60°, and not at all at 50° or less. KCN com
pletely inhibits uricolysis by ox-kidney uricase, whilst Na4P20 7 has no effect. Dog, rabbit, and cat kidneys do not contain uricase. S. S. Zi l v a.
Action of phosphatase on various substrates.
Y. Im a n i s h i (Biochem. Z., 1932, 247, 4 0 6 ^ 17 ).—
Nafructosemonophosphate is hydrolysed to the extent of 80—97% (according to experimental conditions) by phosphatase from A s p e r g illu s o ry zœ and from top and bottom yeast. K diphenylorthophosphate is hydrolysed by takaphosphatase to the extent of 44-5—62-0% and by phosphatase of animal origin (rabbit kidney and liver) to the extent of 35—63%.
W. McCa r t n e y.
Phospho-monoesterase and -diesterase. S.
U z a w a (J. Biochem. Japan, 1932, 15, 19—28).—
Adsorption methods applied to aq. extracts of rice- bran or to solutions of takadiastase yield an enzyme solution which hydrolyses mono-esters but not di
esters of H3P04. The venom of the snake T r im e r e - s u r u s f la v o v ir id is contains a di-esterase with a p a
optimum of 8-6. This enzyme admixed with the mono-esterase from takadiastase hydrolyses com
pletely a di-ester of ELPO., the optimum being at
P u 5-6. F. O. H o w i t t .
Phosphatase from bran. I, II. S. Uz a w a (J.
Biochem. Japan, 1932, 15, 1—10, 11 —17).—I. Rico- bran is extracted with H20, the extract dialysed, treated with kaolin, and the adsorption complex eluted with phosphate buffer to yield a solution of the enzyme which, following dialysis for removal of P04"', is further purified by electrodialysis. This solution contains a phosphatase which hydrolyses various types of mono-esters of H3P04 at an optimum reaction of p a 5-4—5-6. Hence there exist three types of monophosphatases with p n optima at 3, 5-5, and 9, respectively (cf. A., 1929, 847 ; 1930, 372).