In the case of Et| dZ-tartrate the Z-ester is first hydrolysed by both carp’s liver and ox-liver lipases

J. H. B.

Activation of lipases of different origin by polypeptides. E. A b d e r h a l d e n a n d W. G e i d e l

(Fermentforsch., 1932,13,156— 159).—Various leucyl- and glycyl-polypeptides accelerate the action of pancreatic lipase. No relation between activity and structure was observed. Liver-, kidney-, and serum- lipases are not susceptible to activation by these

polypeptides. J. H. B.

Enzym ic form ation of m andelic acid esters.

P. R o n a , R. A m m o n , and H. I. T r t j r n i t (Biochem.

Z., 1932, 247, 100—112).—The influence of strych­

nine, Na taurocholate, MgCL, and CaCl2 on the velocity of formation of Bu mandelate by preps, of human liver and pig’s pancreas is investigated. Strychnine feebly inhibits and MgCl2 greatly accelerates the synthesis.

The products are always optically inactive. In the enzymic esterification of dZ-mandelic acid with dl-

phenylethylcarbinol, the d-carbinol is used more rapidly than the Z-carbinol, whereas the d- and Z- mandelic acids are utilised at the same rate.

P. W. C.

Enzym ic form ation and hydrolysis of esters.

P. R o n a , E. C h a i n , and R. A m m o n (Biochem. Z., 1932, 247, 113—145).—The'prep, and properties of CHPhMe-OII, b. p. 99°/15 min. (b u ty r a te , b. p. 1 1 9 - 123°/14 mm.), CHPliEt-OH, b. p. 100—103713 mm.

(b u ty r a te , b. p. 122—127°/12 mm.), CHPhPra,OH, b. p.

106—109°/12 mm. (b u ty r a te , b. p. 130—140°/14 mm.), and CHPhBivOH, b. p. 139—145°/14 mm. (butyr­

a te , b. p. 139—1450/13 mm.), by the Grignard method and by reduction of the corresponding ketones are described. The butyrates can all be prepared and hydrolysed enzj-mically. In the ester synthesis using pig’s pancreas preps., the d-form is more quickly esterified. The d-form is more readily hydrolysed by pig’s liver preps. P. W. C.

Action of thyroxine on serum -lipase. E.

B a c h , L. L o v a s , and L. N e h f e l d (Arch. exp. Path.

Pharm., 1932, 165, 614^-620).—The tributyrase of rabbit’s serum is reduced by 30—60% after sub­

cutaneous injection of 0-5 mg. of thyroxine andreturns to normal after 3—5 days. Continued daily admin­

istration of thyroxine leads to a reduction in blood- tributyrase which runs parallel with the fall in body- wt., but before death the tributyrase rapidly rises and may even exceed the normal. 17. 0. K.

N uclein m etabolism . XXVI. Nucleophos- phatase. W. K l e i n . XXVH. Enzym ic fission of thym us-nucleic acid w ith nucleotidase from intestinal m ucosa. F. B i e l s c h o v s k y and W. K l e i n ,

XXVIII. Specificity of D isch e’s colour reaction w ith diphenylam ine and carbazole for the purine- and pyrim idine-nucleosides of thymus-nucleic acid. F. B i e l s c h o v s k y and M. S i e f k e n - A n g e r - m a n n (Z. physiol. Cliem., 1932, 207, 125— 140, 202 20.9, 210—212; cf. A., 1930, 1464).—NXVI. A highly active nucleophosphatase was obtained from the intestinal mucosa of the calf. It was purified by pptn. with an AcOH-acetate mixture at p u

and redissolution in alkali. Glycerol extracts of the enzyme may be kept under PhMe without de­

terioration. Glycerol and phosphate and borate buffers inhibit the phosphatase. The Ph optimum is <9-2. Mg salts have an accelerating, action on the enzyme in addition to furthering hydrolysis by

B IO C H E M I S T R Y . 777

pptn. of MgNH4P04. Yeast-nucleic acid is much less readily hydrolysed than that of animal origin.

XXVII. The intestinal enzyme eliminates H3P04 quant, from the nucleic acid mol. and par tly hydrolyses the purine- and pyrimidiuc-nucleosides. Guanosine, thymosine, inosine, and cytidine were isolated from the reaction products. With large amounts of enzyme xanthosine was obtained in small yield.

XXVIII. Both the carbazole and NHPh., reactions of thymus-nucleic acid are due to tliyminose; they are given by the free sugar and all the nucleosides.

Differences in time of appearance are ascribed to differences in stability of the glucoside linking.

J . H. B.

Intestinal nucleotidase and polynucleotidase.

P. A. L e v e n e and R. T. D i l l o n (J. Biol. Chem., 1932, 96, 461—477).—The prep, of the enzyme from gastrointestinal juice of dogs and its properties are described, and the influence of pn on activity towards glyceryl phosphate, adenylic acid, and thymus-nucleic acid is determined. An inhibitor is present in the original secretion. The ratio of nucleotidase to polynucleotidase activity is changed by dialysis, by fractional pptn. with COMe2, and by adsorption, but an attempt: to separate the two enzymes was unsuccessful. The fraction adsorbed appears to be inactivated. Nucleotidase is probably a simple

phosphatase. J. B. B.

Influence of phosphatides on proteolytic enzym es. P. R o n ' d o n i (Z. physiol. Chem., 1932, 207, 103—110).—The process of activation by enterokinase of the tryptic enzymes proteinase and earboxypolypeptidase is inhibited by distearinlecithin, which, however, does not affect tire already activated enzyme. Distearincephalin inhibits the proteinase, but is without action on earboxypolypeptidase.

The phosphatides also inhibit dipeptidase, but not aminopolypeptidase. They accelerate cathepsin activated with H2S or glutathione on a gelatin substrate, but not on clupein. J. H. B.

Action of b lood-serum ,plasm a,and som eorgan extracts on caseinogen and its degradation pro­

ducts. G. E. W i d m a r k (Z. physiol. Chem., 1932, 207, 182—190).—When the proteolytic enzymes in serum, plasma, and organ extracts act on caseinogen and the protein is then pptd., the residual N in the filtrate frequently decreases, indicating a possible resynthesis from the fission products. J. H. B.

Action of spleen enzym es on protein and its fission products. S. G. H e d i n (Z. physiol. Chem., 1932, 207, 213—234).—To show the presence of a- protease in calf spleen the spleen is treated with weak acid and the enzyme is obtained by extraction

(

of the residue with aq. NaCl at slightly alkaline reaction at room temp. The acid destroys an enzyme capable of synthesising protein from its fission pro­

ducts at alkaline reaction. The spleen substance is also hydrolysed by the ¡3-protease, rendering the extraction of a-protease easier. The synthesising enzyme can be obtained from a spleen untreated with acid by extraction with aq. NaCl. When caseinogen, NaCl, and fission products are added to the dialysed infusion, the protein pptd. at the iso­

electric point decreases with time, probably owing

to synthetic action on a substance produced by alkali and NaCl on caseinogen. After 24 In-, at pH 5—5-4 the infusion almost loses its synthetic porver.

With a caseinogen resistant to NaCl the synthesis appears after 4—5 days and the enzyme is more stable to acid. The synthesis' can also be shown with spleen tissue in presence of NaCl and fission products of protein, without added caseinogen. The synthesis is clearer on addition of the synthesising

enzyme. J. H. B.

Production of ereptic action in “ erepsin-free trypsin solutions." E . A b d e r h a l p e n and E . v o n E h r e n w a l l (Fermentforscli., 1 9 3 2 , 1 3 , 2 6 2 — 2 9 0 ;

cf. A., 1 9 3 1 , 7 6 6 ).—The development of the power of hydrolysing dZ-leucylglycine by “ erepsin-free ” trypsin on addition of certain substrates is confirmed.

The following are active in this manner: (a) glycerol -j- NH2-acids, either added as such or pro­

duced by the hydrolysis of complex compounds, (.b) certain sugars + NH2-acids, (c) amino-hydroxy- acids (except (-tyrosine). Tyramine, tyrosineamide, thyroxine, quinine, and particularly chitosamine are also active. The presence of NH2 and Oil groups appears to bo a decisive factor. Inactivated erepsin solutions also stimulate the ereptic action of trypsin.

J. H. B.

P hysical and chem ical properties of poly­

peptides containing glutathione (S-S) and their behaviour tow ards erepsin, trypsin-kinase, and cathepsin. E. Abderhalden and W. Geip e l.—

See this vol., 7-62.

Dehydrodipeptidase. Enzym ic fission of com ­ pounds of pyruvic acid and am ino-acids. M.

B e r g m a n n and H. S c h l e i c h (Z. physiol. Chem., 1932, 207, 235—240).—Phenylpyruvic acid was isolated in 20% yield from the pancreatin hydro­

lysate of glycyldehydrophenylalanine. Kidney ex­

tracts do not hydrolyse glycineamide, which is there­

fore not an intermediate stage. Of pyruvoyl-glycine, -¿(-alanine, and -¿(-phenylalanine, only the last, prob­

ably owing to its higher dissociation const., is hydro­

lysed by pancreatin (optimum p n 7-4). It is not attacked by the proteinase of trypsin. J. H. B.

U rease. I. Separation of urease, its activity and kinetics. A. Ru c h e l m a n n (Biochem. Z., 1932,

247, 8 9 — 9 9 ).—Urease separated by pptn. with EtOH and COMe2 and by means of EtOH after previous pptn. of proteins with HCI is strongly active but preps, obtained by pptn. with AcOH are inactive.

Removal of protein by adsorption on permutite re­

moves also some of the enzyme. The action of urease on urea is catalytic. Changes of concn. of substrate affect the activity of urease, but not the velocity of reaction, changes of urease concn. affect the velocity, but not the activity, and changes of the amount of buffer (pn 7-1) affect the activity and the velocity.

■ P. W. C.

Action of radiation on enzym es. H. B. C o l l i e r

and H. Wasteneys (Austral. J. Exp. Biol., 1932, 9, 89—112).—Ultra-violet radiation (200—313 mg) de­

stroys impure urease, malt amylase, pepsin, and plasma-phosphatase, whilst the urease is also de­

stroyed by infra-red radiation (750—1400 mg) and the phosphatase by visible radiation. Visible radiation

778 B R I T I S H C H E M IC A L A B S T R A C T S .— A .

stimulates starcli-amylase digests slightly and pepsin- ovalbumin digests strongly, although it has no effect on the enzymes alone. Probably the colloidal sub­

strate of the digests absorbs the radiations, the energy of which is then degraded to the kinetic form with consequent increase in the rate of reaction. The rate of destruction of pepsin by ultra-violet radiation de­

pends on the [H‘] within the range p K 1—7, the point of max. destruction coinciding with that of optimum

activity of the enzyme. W. M.

Source of heat in anaerobic energy-producing reactions. C. N e u b e e g and E. H o f m a n n (Natur- wiss., 1932, 20. 379—3S1).—Thermochemical data show that there is little energy change in the con­

version of glucose into methylglyoxal, but that the dismutation of the latter into EtOH and C02 or lactic acid is responsible for the heat produced in alcoholic or lactic acid fermentation. A. C.

Stability of glycolase. C. N e u b e r g and M.

K o b e l (Austral. J. Exp. Biol., 1 9 3 2 , 9 , 1 27— 1 3 3 ).—

Yeasts (37 preps, tested) which have been preserved for periods up to 20 years produce methylglyoxal from Mg hexosediphosphate but do not ferment sugar after addition of co-enzyme. W. M.

Adenosinetripbospboric acid and cozym ase.

H. v o n E u l e r and R. N i l s s o n (Z. physiol. Chem., 1932, 208, 173—1 S 1 ).—Cozymase and adenosinetri- phosphoric acid (as Ca salt) activate lactic acid form­

ation in muscle juice to an approx. equal extent ; in some cases the cozymase is superior, but never inferior, contrary to Lohmanirs finding (A., 1931, 1449). The main action of the adenosinetriphosphate may be to shorten the induction period, cozymase probably being present as impurity. J. H. B.

Behaviour of i-histidine in y east ferm entation.

W. Keil (Z. physiol. Chem., 1932, 207, 275—276).—

Added histidine disappeared rapidly in a yeast fermentation, but no histidol could be isolated.

J. H. B.

Stim ulation of yeast grow th by thallium ; a

“ bios " im purity of asparagine. O. W. R i c h a r d s

(J. Biol. Chem., 1932, 96, 405— 418).—The wide variations in the growth of yeast in a medium when different- brands of asparagine were used is accounted for by the presence of T1 which in concns. of 0 001 mg. per c.c. of medium produces an increase of 80%

in the vield of yeast; greater concns. are toxic.

H. D.

Action at a distance of m etals on bacteria and yeast. G. A. N a d s o n and C. A. S t e r n (Compt. rend., 1932, 194, 1597—1600).—The growth of certain bacteria and of yeast in Petri dishes is to some extent inhibited by the presence of certain metals near the surface of the medium, but not in contact with it, the order of activity being Pb>Cu>Al. W. 0. K.

Chem ical com pounds lethal to yeasts and bacteria. W. N e w t o n and H. I. E d w a r d s (Sci.

Agric., 1932, 12, 564—567).—Data for a number of substances are given. The higher PhOH-coeff. of KMn04 offers an explanation of its action in in­

creasing the fungicidal efficiency of S dusts.

A. G. P.

Phenom enon of B oas [action of thiocyanate on m icro-organism s]. P. L a s s e u r , A. D u p a i x , and

L . G e o r g e s (Compt. rend., 1932, 194, 1857^— 1859).

—The fixation of Bordeaux B in presence and absence of KCNS by bacteria (B . c a ry o c y a n e u s ) and by a basidiomyeete (M o n ili a a lb ic a n s) at various reactions was investigated (cf. A., 1926, 1276). With B . caryo- c y a n e u s the bacterial vol. has a min. at p n 3-6.

Addition of KCNS induces a decrease in the swelling and in adsorption of the dye at any reaction. The min. of swelling corresponds with max. adsorption of dye whether KCNS be present or not. M . albicans

has a min. vol. at p H 3-0 and, in presence of KCNS, at p K 3-4. In contradistinction to the bacteria, presence of KCNS increases the adsorption of dye over a range of p a 2-4—8. The fixation of dye in various buffer solutions, with and without KCNS, indicates the importance of anions. E . 0. H.

Soluble enzym es secreted by H y m e n o n i y c e t e s .

Ketones, anthraquinones, and antioxygenic func­

tion. L. L u t z (Compt. rend., 1932, 194, 1684—

1686).—Various ketones were tested for antioxygenic activity on methylene-blue in presence of certain

B a s id io m y c e te s with negative results. Anthraquinone also exhibited no antioxygenic action, but a well- marked action was shown by hvdroxyanthraquinones.

F. O. H.

Reactions of Lindner's T e r m o b a c t e r i u m 7 n o b i l e . C. N e u b e r g and M. K o b e l (Bioehem. Z., 1932,247,246—248) .—The bacterium converts AcCHO and BzCHO into the corresponding a-OH-acids, the yields being 87% of d ( —)-laetic and 86% of d ( —)- mandelic acids. Since isolation of the products is not quant., the dismutation must be asymmetric and almost complete (cf. this vol., 195). P. W. C.

Tem perature characteristic of respiration of

A z o t o b a c t e r . H . L i n e w e a v e r , D . B u r k , and C . K . H o r n e r (J. Gen. Physiol., 1932, 15, 497—505).- The crit. thermal increment of A . v in e la n d ii has a const, val. of 19,330 between 20° and 30°. This val.

is independent of p R, 0 , pressure, and age of culture.

The optimum temp, of respiration is 34—35' with limits at about 10° and 50°. A. L.

Therm ophilic nitrite form er. E. G. ^{C a m} p b e l l

(Science, 1932, 75, 23).—A new organism which oxidises NH4 salts to nitrite at 55° in amounts from 1 to 5 parts of nitrite-N per million is described.

At p n 9-4 oxidation is at a max., at p B 6-3 it is slight, and at p s 4-S it ceases. 1% of glucose added to the mineral salt medium completely inhibits nitrite formation, 0-5—0-25% retards it, but 0-1% has no effect ; 1% of peptone checks oxidation temporarily.

Free C02 from the atm. is necessary as the source of C. NH4 salts are always used as a source of energy, except when starch is added to the inorg. salt medium.

The suggested name is _Yitro so b a c illu s thennophilu-s,

Campbell. I*. S. T.

Production of a cyanogen radical in peptone w ater cultures of cholera vibrio. C. L . P a s r i c h a

and S. M. D a s - G u p t a (Indian Med. Gaz., 1931, 66, 551—552).—CN' was found after incubation for 72 hr. at 37°, acidification with tartaric acid, and distillation into KOH solution. Faeces from cholera.

B IO C H E M I S T R T . 7 7 9

when distilled, gave the AgN03 reaction of CN'. S . dysenteries (Flexner and Shiga), E . ty p h i , and E . coli

gave negative results. Ch. Abs.

B . c a r y o c y a t i e u s (Beijerinck-Dupaix) in a medium containing lithium. P. L a s s e u r , P.

V e r x i e e , A. D u p a i x , and J. M a r c h a l (Compt. rend., 1932, 194, 1606—1608).—The presence of Li in a medium in which B . c a r y o c y a n e u s is grown induces morphological changes associated with alterations in the permeability of the bacterial membranes and in the stability of suspensions of the bacteria in presence of cations or of agglutinating serum. W. 0. K.

Nucleic acid of B . d i p h t h e r i a ; . R. D. C o g h i l l

and D. B a r x £ s (Anal. Fis. Quim., 1932, 3 0 , 208—

221).—A nucleic acid was obtained in 0-8% yield by extraction of B . d ip h th erice with 2% NaOH (cf.

A., 1931, 526). The approx. composition is N 14-5, P 8, guanine 9-5%, and it yields on hydrolysis guanine, adenine, cytosine, uracil, and thymine. It contains at least 13% of pentose, and 25% of nucleic acid of animal type is indicated by Widstrom’s method (A., 1928, 1393). It is, therefore, either a new type or a mixture of plant and animal types. R. K. C.

Relation between toxicity and antigenic potency of diphtheria toxins. G. S t o d e l and A.

B o u b d d t (Compt. rend., 1932, 194, 1687—1688).—- The relation of the antigenic potency (y) of a diphth­

eria toxin measured in definite units (A., 1924, i, 463) to the toxicity (x) measured in min. lethal doses for the guinea-pig is expressed by y = K x2, where K

is a const.—6-3. F. 0. H.

Cryptotoxic properties of sodium a-hydroxy- P-naphthoate and its selective action on diphth­

eria toxin. H. V i n c e n t and L. V e l l u z (Compt.

rend., 1932, 194, 1697—1699).—The salt detoxicates tetanus toxin, injection of the cryptotoxin thus formed inducing complete immunity' in the guinea-pig. It also neutralises diphtheria toxin, subcutaneous injec­

tion of diphtheria cryptotoxin being well tolerated by the guinea-pig, which is thereby rendered com­

pletely immune. Thus a guinea-pig injected with 5-5 c.c. of neutralised toxin can receive 12,500 times the min. lethal dose of toxin without the occurrence

of abnormal symptoms. F. 0. H.

Use of ethyl alcohol as precipitant in the con­

centration of anti-pneumococcus serum. L. D.

F e l t o n ( J . Immunol., 1 9 3 1 , 2 1 , 3 5 7 — 3 7 3 ).—Prac­

tically all the protective substance is insol. in 15—2 0 %

EtOH at 0 ° .. The H20-insol. protein is dissolved in NaCl solution and pptd. with 1 0 % EtOH, giving a product in which the immune protein is approx.

8 0% of the total protein. Between p B 5 and 9, if the ppt. is neutralised before dilution, the pneumo­

coccus antibody' is insol. in 2 0 % EtOH. C h . A b s .

Gas m etab olism of the tubercle bacillus. I.

Oxygen consum ption. H. ^D i e c k h a x n and G.

Me x z e l ( Z . Hyg., 1 9 3 2 , 1 1 3 , 7 0 9 — 7 3 4 ) . —The 02- consumption of human strains v'as 20 cu. mm. per mg. dry wt. per hr., corresponding with 57-5 g.-cal.

per g. N per 24 hr. In NH4OAe-phosphate buffer suspension the 0 2-eonsumption was 3—4 times that in NaCI, Ringer, or phosphate buffer solutions

without NH.OAe. . A. G. P.

3 F

Molecular weight of specific polysaccharides.

M. He id e l b e r g e r and F. E. Ke n d a l l (J. Biol.

Chem., 1932, 96, 541-—558).—Staudinger’s procedure for determining mol. wt. of the higher members of a series of polyunerides by' viscosity measurements is applied to the ty'pe III pneumococcus sp. poly­

saccharide, the lower polymerides being obtained by hydrolysis. The apparent mol. wt. varies with salt concn. of the solution, but correction for hy'dration gives a val. of approx. 1000. The diffusion method, assuming spherical particles and similarly' corrected for hy'dration, gives 5600. Diffusion data are given for bovine tubercle bacillus polysaccharide, and it Is concluded that the formula w'ts. of the sp. poly- saccharides should be less than 10,000. J. B. B.

Resistance of guanidine and alkylated guan­

idines to bacterial guanidodeimidase and arginase. F. Lixnew eh (Z. physiol. Chem., 1932, 207, 152— 156).—Guanidine and alkvlguanidines are not attacked by' mixed cultures of putrefactive bacteria and are therefore resistant to guanidode­

imidase and arginase. In boiling aq. solution guanidine carbonate forms urea. This may explain

Ackermann’s observation (A., 1909, i, 619).

J: H. B.

Bacterial multiplication. M. ^{Fa g u e t} (Compt.

rend., 1932, 194, 1763—1764).—The growth of various bacteria in homogenous emulsions results in an increase of opacity' which can be followed by utilisation of a photo-electric cell (this vol., 545).

For the same experimental conditions the curves thus obtained are sp. for each distinct species.

F. O. H.

Biochemistry of the cortex of the suprarenal gland. I. Preparation and detection of the hormone of the suprarenal cortex, H. ^{Ma g istris} (Biochem. Z., 1932, 248, 39—54).—Two methods for preparing an aq. solution of the hormone are described, and the activity' is demonstrated by' maintaining suprarenalectomised rabbits alive. For the extract to be effective, it must be administered to the animals before extirpation of the glands. The hormone unit is suggested as the smallest amount which with daily subcutaneous injection is able to maintain suprarenal - ectomised rabbits alive for 1 week, the administration starting 2 days before the gland removal. P. W. C.

Hyperglycaemic activity of extracts of supra­

renal cortex. M. T. Re g x ie r and H. Sim o nne t

(Bull. Soc. Chim. biol., 1932, 14, 614—622).—Supra­

renal cortex is ground with H20 and the paste ex­

tracted with 10 vols. of 95% EtOH. The extract is conc. to dryness in vac., the residue dissolved in PhMe, phospha tides are pptd. by COMe2, and the filtrate is again conc. to dry'ness. The oily' residue dissolved in petrol is freed from adrenaline by washing with dil. alkali, dried, and evaporated to dry'ness, giving a residue sol. in olive oil. Injection into dogs of amounts equiv. to 2—20 g. of fresh gland produces a marked hyperglycajmia characterised by' long duration of action which is not due to adrenaline. F. 0. H.

Nervous mechanism of adrenaline action on muscle-glycogen. C. ^Br e n t a n o (Arch. exp. Path.

Pharm., 1932, 165, 494—503).—In rabbits the muscle-glycogen disappears after administration of

780 B R I T I S H C H E M IC A L A B S T R A C T S .— A .

adrenaline even though the mixed nerves proceeding to the muscles have previously been cut. Although this indicates that the action is not dependent on impulses passing down these nerves, it does not prove that the action is directly on the muscles themselves.

W. 0. K.

Colloid-chemical basis of inflammation pre­

vention by adrenaline. F. Hin t e r e g g e r (Z. ges.

exp. Med., 1931, 78, 374—381; Chem. Zentr., 1931, ii, 3623).—Addition of adrenaline hydrochloride to serum or to gelatin solution alters the viscosity only in so far as p a is changed by the addition. The colloidal osmotic pressure of horse serum is also unchanged by adren­

aline. A diminution of the swelling pressure of the serum-colloids cannot be assumed as the cause of the prevention of inflammation bv adrenaline.

L. S.T.

Alleged increase in plasma-fat after injection of adrenaline. C. N. H. Long and E. M. Ve n n i n g

(J. Biol. Chem., 1932, 96, 397—404).—Injection of adrenaline does not produce an increase in plasma- fats in cats but an increase in blood-sugar. H. D.

Effect of adrenaline on tbe blood-cholesterol and -cbolesteryl ester in relation to blood pres­

sure and blood-sugar. K. ^Gu g g e n h e im (Z. klin.

Med., 1931, 116 , 717—731; Chem. Zentr., 1931, ii, 3623).—A regular change in blood-cholesterol did not result from the injection of adrenaline. L. S. T.

Tbymus and suprarenal medulla in regulation of blood-cholesterol. A. ^Poli(Arch. Farm, sperim., 1932, 54, 44—54).—Adrenaline and thymus extract have opposite effects on blood-cholesterol in rabbits.

Tbymus and suprarenal medulla in regulation of blood-cholesterol. A. ^Poli(Arch. Farm, sperim., 1932, 54, 44—54).—Adrenaline and thymus extract have opposite effects on blood-cholesterol in rabbits.

W dokumencie British Chemical Abstracts. A. Pure Chemistry, July (Stron 110-114)