Organic Chemistry
X- Ray investigations on stimulated and para
lysed nerve substance. H . Ha n d o v s k y (Kolloid- Z., 1933, 62, 21— 22).— The nerve substance of a frog narcotised with CHC13 gives interference rings which agree with those obtained from Na oleate. It is probable that orientation of fatty acid mols. occurs
during narcosis. E. S. H .
X - R a y d i a g r a m o f n e r v e s . G. Bo eh m (Kolloid- Z., 1933, 62, 22— 26).— A review, demonstrating how far the fine structure of nerves can be recognised by X-ray analysis, and the changes brought about by narcosis and degeneration. E. S. H.
Biological effects of high pressure : resistance of bacteria, enzymes, and toxins to very high pressures. J. Ba sse t and M . A. Machebceuf
(Compt. rend., 1932, 195, 1431— 1433).— Bacteria generally survive exposure to a pressure of 3000 atm.
in liquid media at p n 6-9— 7-2 for 45 min. B. prodigio- sits, S. aureus, and Koch’s bacillus are rapidly de
stroyed at 6000 atm. Sporing bacilli (B. subtilis) resist 17,600 atm. for 45 min. Enzymes are only partly inactivated below 9000 atm. Above this pressure inactivation is rapid. Diphtheria toxin loses 80% of its activity in 45 min. at 13,500 atm. and all at 17,600 atm. Tetanus toxin is slightly more sensitive. Cobra venom and tuberculin are not affected by 13,500 atm. for 45 min. A. C.
Flocculation of colloidal dyes in the organism.
M. Pie t t r e (Compt. rend., 1933, 196, 298— 300).—
Various electro-positivo, colloidal dyes, when injected intravenously into rabbits, are pptd. in various organs, the organ affected being to a certain extent sp. for the dye used. Electro-negative dyes are usually
without effect. R. S. C.
New oxidation enzyme. 0 . Wa r b u r g and W . Ch r is t ia n (Naturwiss., 1932, 2 0 , 980—981).—A summary account of the isolation of a new oxidation enzyme from ycast-juico. The enzyme, consisting of protein coupled with pigment, shows absorption bands at 435, 465 (max.), and 495 mjr. The free pig
ment, with absorption shifted 15— 20 mix towards the blue, crystallises from H 20 in needles. R. K . C.
Catalytic deamination of amino-acids. B.
Ki s c h.— See this v ol., 263.
Quinones as enzyme models. VIII. C 0 2/NH3 quotient in oxidative deamination. B. Kisc h and K. Sc h u w ir t h (Biochem. Z., 1933, 257, 89— 94).
— In the oxidative deamination of glycine (I) and serine in presence of catalysts (pyrocatechol, hydroxy - quinol, adrenaline, gallic acid, resorcinol) C02 and NH3 are eliminated in the ratio 1 : 1, but when glycylglycine (II) and glycyltyrosine are similarly
y*
deaminated with hydroxyquinol as catalyst no C02
is produced. Traces of C02 which are produced with (II) and the greater amount obtained with glycine Et ester probably come from small amounts of (I) liberated by hydrolysis. Only traces of C02 and NH3
are obtained with alanine, leucine, and fsoleucine.
In theso experiments borate can replace phosphate
as buffer. W. McC.
Peroxidases. II. Influence of concentration of substrate (quinol), hydrogen peroxide, and other factors on activity of peroxidase of Chow Chow (Sechium edule). B. B. De y and M. V.
Sit h a r a m a n (J. Indian Chem. Soc., 1932, 9, 499—
508).— The activity of the enzyme is dependent on the concn. of II202 and quinol, and p a, being greatest at p s 4-8— 5-2, and completely suppressed in presence of sufficient HC1. It is very readily poisoned by KCN, but is less sensitive to HgCl2. H. A. P.
Biological hydrogenation of fumaric acid under the influence of cereals. K. P. Ja c o b s o h n
and A. d a Cr u z (Compt. rend. Soc. Biol., 1931, 107, 94— 96; Chem. Zentr., 1932, ii, 1S00).—When ground rice, maize, oats, etc. which has been treated
* with COMe2 and E t,0 is added to 2% aq. fumaric acid neutralised with KOH, emulsified, and kept at 37°, malic acid is gradually formed. A. A. E.
Kinetic study of liquefaction and enzymic saccharification of starch. I I . Pancreatic amyl
ase. G. Or e s t a n o (Bull. Soc. Cliim. biol., 1932, 14, 1531— 1551).— Liquefaction of starch with pancreatic amylase behaves as a unimol. reaction. Saccharific
ation follows this law at high concns. of enzyme only. The rate of liquefaction runs parallel to the amount of enzyme present and is directly propor
tional to the concn. of the substrate ; the rate of saccharification is directly proportional to the amount of the enzyme and is inversely proportional to the concn. of the substrate. H. G. R.
Determination of the starch-liquefying power of amylase. T. Chrzaszcz and J. Ja n i c k i (Bio
chem. Z., 1932, 256, 252— 291).— Determinations of the starch-liquefying power -with malt amylase (from rye, wheat, oats, barley) were carried out, using 15 known methods and 21 published modific
ations thereof. Seven of the methods gave trust
worthy results, and the peculiar advantages of each are given. In order to obtain comparable results it is necessary to specify the methods of preparing both starch and enzyme. The liquefying power of amylase from the different cereals is very different. Dis
placement of the pa of the starch to 5 increases the sensitivity of all the methods. P. W. C.
Amylolytic fermentations. TV. Influence of diamines and their hydrochlorides on the sac
charification of starch by pancreas, saliva, and malt extract. E. Ca u j o l l e and P. Ro ch e (Bull.
Sci. pharmacol., 1932, 39, 361— 372; Chem. Zentr., 1932, ii, 2666).— Ethylenediamine, putrescine, and cadaverine inhibit the amylolytic action in each case. The hydrochlorides have no effect on that of malt extract, scarcely affect that of pancreas, and increase that of human saliva. A. A. E.
314 B R IT IS H CHEM ICAL A B STR A C T S. A .
3-Glucosidase. C. Nb u b e r g and E. Ho f m a n n
(Biochem. Z., 1932, 256, 450— 461).— Enzyme solutions prepared from the lactose fermenters Saccha- romyces fragilis, S. Kefir, and lactose-yeast, Sp. 102, hydrolyse not only p-galactosides in the wide sense (lactose, lactoseureide, lactobionic acid) and (3-methyl-, (3-ethyl-, and (3-phenyl-galactosides, but also the (S-glucosides amygdalin, (3-methylglucoside, salicin, arbutin, and cellobiose, but do not attack melibiose (which is hydrolysed by emulsin). Enzymic hydro
lysis and power to ferment by the fresh yeast do not always run parallel, and the (3-glucosidase of these enzyme solutions is different from that of emulsin.
P. W. C.
(3-Glucosidase of lactose fermenters. E. Ho f m a n n (Biochem. Z., 1932, 256, 462— 474).— Whereas emulsin lactase is considerably inhibited by glucose and little by galactose, the reverse is true of the lactase of enzyme aolutions from S. Kefir, and whereas the 2hi optimum for the former is 4-4, for the latter it is 7. The rate of hydrolysis with kefir lactase is the same for lactose and for lactoseureide. Optimum hydrolysis of salicin and (3-methylglucoside is at pa 6, activity decreasing rapidly on both sides. Only against amygdalin have both emulsin and the enzyme' solutions a wide p R optimum. The reaction with (3-glucosidase of the enzyme solutions is not unimol., as is the action of emulsin on (3-glucosides. From the aq. enzyme solutions a dry prep, is obtained, by an E t0 H -E t20 method, which possesses hydrolytic activity of both p-galactosides and p-glucosides.
The optimum is 6, and it forms the most active
lactase prep, known. P. W . C.
Enzymes of the mammary gland. Presence of glucomaltase. I. S. Kl e in e r and H. Ta u b e r (J. Biol. Chem., 1932, 99, 241— 247).— Glycerol extracts of cows’ mammary glands contain no pro- tease, salolase, lactase, or amylase. A maltase is present which hydrolyses maltose but not a-methyl- glueoside or sucrose, and has a p a optimum of 6-8— 7-0. Comparison with other maltases indicates the existence of glucomaltases as distinct from glucos- idomaltases (A., 1926, 322, 865). F. 0. H.
Reactivation of koji-invertase. N . Ta k e t o m i
and T. Ho r ik o si (J. Soc. Chem. Ind., Japan, 1932, 35, 583b).—The activity of koji-invertase (I) that has been injured by very dil. (e.g., 0-0 1AT) acids or alkalis can be gradually and partly restored by cold storage after neutralisation. (I) damaged by strong alkali, acids, or heat does not recover. HgCL, has a marked action on (I), but the activity is com pletely restored by passing H2S through the solution.
E. L.
Dismutation of glyoxal. C. Ne u b e r g and E.
Sim o n (Biochem. Z., 1932, 256, 4 8 5 -4 9 1 ).— The extent of dismutation of glyoxal to glycollic acid is followed, using enzyme solutions prepared from pea seedlings, pig’s liver and kidney, rabbit liver, COMe2- dried pea preps., and bottom and top yeast.
P. W. C.
Iodoacetic acid, glutathione, and tissue glyoxal- ase. F. Dic k e n s (Nature, 1933, 131, 130— 131).—
With extracts of rat liver purified by isoelectric pptn. and dialysis, or with undialvsed extracts, the
action of CH2I-C02H (I) in arresting glyoxalase (II) activity is completely reversed by the addition of reduced glutathione (III) to the inhibited extract.
In a dialysed extract activated by glutathione (III) the quantity of iodoacetate (IV) required to stop lactic acid formation is approx. equiv. to the (III) added. The (II) activity of the crude extract is unaffected by such a concn. of (IV) and requires a much larger amount before lactic acid formation is arrested or retarded. The results suggest the occur
rence of a direct reaction between (III) and (I), which has been observed when dil. neutral solutions of acid and (III) are mixed. H I is liberated and the thiol group of the (III) is attacked. L. S. T.
Chemical biology of growth-promoting sub
stances. I. Enzymes of the extract of the embryo chick. G. Borger and T. Pe t e r s (Z.
physiol. Chem., 1933, 214, 91— 103).— The embryonal extract (I) contains dipeptidase, less aminopoly- peptidase, a trace of proteinase, amylase, and lipase.
The activity of the dipeptidase falls by about 90%
and that of the polypeptidase by about 50% in 50 days at 0°. The yolk membrane in glycerol extract contains about 1 2 times as much as (I) (glycerol extract), allantois only 1/5. The enzyme content of the incubated egg varies within wide limits.
J. H. B.
Nature of emulsin, rennin, and pepsin. H.
Ta u b e r (J. Biol. Chem., 1932, 99, 257— 264).—
Emulsin is prepared by extraction o f fat-free almond meal with 33% EtOH and pptn. of the extract by addition (1 : 1) o f 96% EtOH. The prep, is in
activated by acid (pa < 2), but not by pepsin, trypsin, or pancreatin. Active preps, o f emulsin, rennin, and pepsin, however purified, give positive protein tests when sufficiently conc., but not when considerably diluted, a finding which refutes evidence for the non
protein character o f these enzymes. F. 0 . H.
Action of rennin on caseinogen. M. Be a u
(Lait, 1932, 12, 618— 640; Chem. Zentr., 1932, ii, 1984).— Rennin is considered to catalyse the poly
merisation o f caseinogen with the aid o f CaO and
H3P 0 4. A. A. E.
Enzymic formation of acetoin. II. From proteins. W . Ciu s a (Annali Chim. Appl., 1932, 22, 747— 753 ; cf. A., 1932,1287).— Acetoin is formed by the action of pepsin, trypsin, or papain on milk, blood- serum, or egg-white, in the last case from the ovo
mucoid. T. H. P.
Properties of proteolytic protective enzymes.
Optimal p „ of their action. Detection of poly
peptidase in urine. E. Ab d e r h a l d e n and S.
Bu a d z e (Fermentforsch., 1932, 13, 363— 381).— The optimal p R for the action o f the protective enzymes of the urine and serum o f pregnancy and o f animals previously injected with placental peptone is 7-0 for a protein substrate, 7-5 for JZ-leucylglycine. With a peptone substrate max. activity is observed both below and above p H 7-0. The polypeptidase activity of serum and urine is enhanced by the appearance of protective enzyme. Their inactivation by chilling, activation by serum, and specificity distinguish the protective enzymes from other proteases. A. C.
BIO CH EM ISTR Y . 315
Enzyme systems contained in erepsin- and trypsin-complex. E. Ab d e r h a l d e n and W. Ze is- s e t.— See this vol., 265.
Behaviour of polypeptides composed solely of Z(+)-a-aminobutyric acid towards N alkali, erepsin, and trypsin-kinase. E. Ab d e r h a l d e n
and E. Ha a s e.—See this vol., 264.
Behaviour towards erepsin and trypsin of polypeptides containing a-aminoisobutyric acid.
E. Ab d e r h a l d e n and W. Ze is s e t.— See this vol., 264.
Physical properties of polypeptides composed of i(-)-)-norleucine and their behaviour towards erepsin and trypsin. E. Ab d e r h a l d e n and K.
Pl o t n e r.— See this vol., 264.
Identity of the chloroacetyl-i-alanine-splitting component of erepsin solutions with that which hydrolyses chloroacet-o-nitroanilide and related compounds. E. Ab d e r h a l d e n, E. v o n Eh r e n- w a l l, E. Sc h w a b, and 0. Zh m st e in (Fermentforsch., 1932, 13, 408— 432).— Trypsin-free preps, of erepsin which hydrolyse chloroacetyl-Z-alanine do not hydro
lyse chloroacet-o-nitroanilide (I). Hydrolysis of the latter, for which p a 8 - 0 is optimal, occurs only when trypsin is incompletely removed. The acylase of erepsin (A., 1931, 125) is therefore not identical with the ereptic enzyme described by Balls and Kohler (A., 1931, 521), which hydrolyses (I). Preps, of the latter enzyme are inactive towards chloroacetyl-cZZ- leucine, chloroacctyl-Z-tyrosine, and benzoyltriglycine.
(I) is hydrolysed by enzymes of liver and urine, but not by pancreatic extract. The activity o f erepsin and trypsin towards m- and p-nitroanilides is con
siderably lower than towards the o-isomerides. Erep
sin also hydrolyses chloroacet-o-toluidide, m.p. I l l —
1 1 2°; chloroacetanilide, dl-a.-bromopropion-o-nitro- anilide, m.p. 64— 65°; chhroacet-o-chloroanilide, m.p.
75— 76°; and o-nitro-oxanilide Et ester, m.p. 108°, but not chloroacet-p-toluidide, 2 : 2'-dinitro-oxanilide, m.p. 326°, N-o-nitrophenylphthalimide, m.p. 199°, chloroacetylaminoacrylic acid, phthalylglycyl-, and phtlialyldiglycyl-glycine, m.p. 239°. A. C.
Influence o f thiol com pou n ds on enzym ic processes. E. Wa l d s c iim id t-Le it z, A. Sc h a r i- k o v a, and A. Sc h a f f n e r (Z .physiol. Chom., 1933,214, 75—8 8).— Cathepsin freed from natural activator becomes active towards proteins only in presence of a thiol compound, e.g., cysteine, which likewise activ
ates papain. Arginaso is activated by SH and Fe"
salt under conditions in which SH alone inhibits.
Cysteine or H 2S specifically inhibits the hydrolysis of H3P 04 esters induced by phosphatase, but does not appreciably affect their synthesis; disulphide com
pounds such as cystine are inactive. This also applies to the elimination o f H3P 04 from nucleic acid by nucleotidase. SH-compounds inhibit catalase, in part irreversibly, but the degree of inhibition depends on the contact time and is not instantaneous as with HCN.
Cystine shows no inhibition. P 0 4'" , A s O /", citrate, and EtOH depress the action o f SH compounds on
catalase. J. H. B.
Tumour-arginase. II. Activation and in
hibition of arginase. III. Action of boiled and
native juices from tumour, muscle of the affected animal, and from healthy muscle on arginase from liver and tumours and on extracts from healthy muscle. G. Kl e i n and W. Zie s e (Z.
physiol. Chem., 1932, 213, 201— 216, 217— 225; cf.
A., 1932,1167).— II. The liver-arginase (I) o f man and other mammals behaves like calf’s liver-arginase towards thiols. In dil. suspensions and extracts cysteine and glutathione behave as inhibitors. Liver - and tumour-arginase (II) from carcinomatous subjects frequently show activation effects. This is not due to a direct effect on the enzyme, but to interaction between the thiols and the other substances present.
When thèse are removed the thiols produce inhibition.
The hypothesis of the action of Cu or simple Cu com
pounds does not satisfactorily explain the facts.
III. Boiled juices o f tumour extracts strongly inhibit (I) and (II), but have no action on inactive muscle extracts of healthy animals. Only cone, boiled juices from healthy and diseased muscle in
hibit, dil. native extracts slightly activate, and cone, strongly inhibit (I). The inhibitors are degradation products o f protein metabolism. J. H. B.
Ammonia production during the histamine- histaminase reaction. E. W. McHe n r y and G.
Ga v in (Trans. Roy. Soc. Canada, 1932, [iii], 26, V, 321— 328).— Histamine (I), when acted on by a histaminase prep, from pig’s kidney (A., 1932, 92) in P 0 4"'. buffer at p „ 7-2 or 8 - 8 and at 38°, liberates 1 N as NH3 for each mol. o f (I) inactivated. At p a 5-9 the amount of NH3 is considerably less. Tins formation of NH3 is due to deamination, which at certain reactions is also accompanied by rupture o f the glyoxaline ring. Urea is not formed. F. O. H.
Lipases of wheat. I. B. Su l l iv a n and M. A.
Ho w e (J. Amer. Chem. Soc., 1933, 55, 320— 324).—
Triacetin (I) is hydrolysed to a greater extent by low-grade flour than by bran or germ in phosphate or phosphate-borato buffers at 37-9° for 24 hr. ; optimum activity is at pn 7-3— 8-2. Hydrolysis of the higher glycerides does not occur so readily and the optimum is on the acid side. Germinated wheat has a higher lipase activity towards the higher glycerides, but not
towards (I). H. B.
Action of pancreatic extract on glycine in glycerol medium. R . Wolffand (Ml l e.) La f r a n- ca ise (Compt. rend., 1933, 196, 221— 223).— A slow and irregular decrease in the no. of C02H groups occurs when a 3% solution of glycine in glycerol is incubated at 37° with pancreatic lipase (hog). In presence of EtOH a marked decrease is observed, reaching 20— 30% at p a 5— 9 in several weeks, in
dicating estérification of glycine. A. G.
Choline-esterase, an enzyme present in the blood-serum of the horse. E. St e d m a n, (Mr s.) E. St e d m a n, and L. H. Easso n (Biochem. J., 1932, 26, 2056— 2066).— The enzyme hydrolyses acetyl- and butyryl-choline, Me butyrato (I), and tributyrin (II). It can bo purified by fractional pptn. with (NH4)2S04. The activities towards (I) and (II) are much depressed in purified preps. S. S. Z.
Phosphatase. I. Determination of inorganic phosphate. Beer’s law and interfering sub
316 B R IT IS H CHEM ICAL A B STR A C T S.— A .
stances in the Kuttner-Lichtenstein method.
A. Bo d a n s k y (J. Biol. Chem., 1933, 99, 197— 206).—
The Kuttner-Liehtonstein procedure (A., 1930, 725) is modified by making up the standard Na molybdate solution from molybdic acid and NaOH and by using a SnCl2 solution containing 60 g. in 100 c.c. conc. HC1.
The deviation from Beer’s law produces a 20% differ
ence between the vals. found for the concns. of the unknown and the standard ; a table of corr. vals. may he used. The conditions of the test are standardised to obviate the largo errors entering when CCl3-CO,H or CC13-C02H -f- glycerophosphate is present as in serum-inorg. P and phosphatase determinations.
H. D.
Paradoxical increase of phosphatase activity in preserved serum. A. Bo d a n s k y (Proc. Soc.
Exp. Biol. Med., 1932,29,1292— 1293).— Blood-serum kept for 1 hr. at room temp, and 23 hr. at 0° showed an increase (7— 23%) in phosphatase activity; inorg.
P was unchanged. Ch. Ab s.
Decomposition of adenylpyrophosphate in vitro. E. Ja c o b s e n (Biochem. Z., 1933, 257, 221—
233).— In inactivated, feebly alkaline (pa 9-2— 10) muscle extracts more equivs. of NH3 than of pyro
phosphate are eliminated, whereas in neutral or feebly acid extracts the ratio is 1 : 1 . Deamination and dephosphorylation are independent and the former proceeds 2 0 times as fast with adenylic acid (I) as with adenylpyrophosphate (II). NaF, CH2I-C02Na, and KCNS (but not KCN) restrict or inhibit the conversion of (I) into (II) as they restrict or inhibit production of lactic acid. W . McC.
Hexose monophosphoric esters : mannose monophosphate. R. Ro b is o n (Biochem. J., 1932, 26, 2191— 2202).— A third component— monophos
phoric ester of mannose, [a]™,u -f-15-10 (Basalt, [a]fj01 + 3-5°; phenylhydrazine salt of phenylhydrazone, m.p. 144— 145°; phenylhydrazine salt of osazone, m.p. 154— 155°)—has been isolated from hexose mono
phosphate produced by fermentation of hexoses with yeast-juice. The Hagedorn and Jensen reducing power of the ester is the same as that of glucose and fructoso monophosphate. The I-reducing power is only 60— 70% of the val. theoretically required for an aldose monophosphate. It is very slowly hydrolysed by iV-HCl at 100° ( X = 0-29x10-% The rate of hydrolysis of the free ester in 0-0 1JJi solution is the same as in N-HC1. Neuberg’s fructoso monophos
phate has been isolated in a purer form as a com
ponent of fermentation (A., 1931, 523). In A7-HC1 the val. of K for this compound is 4-36 X10-3, but in 0-OlJf-solution of the free ester the initial val. of K
is 0-37 X lO-3. S. S. Z.
Relation, of thiol compounds to glucose fer
mentation. J. H. Qu a s t e land A. H. M. Wh e a t l e y
(Biochem. J., 1932, 26, 2169— 2176).— CH2I-C02H reacts with Na2S20 3, cysteine (I), and glutathione (II).
(I) and (II) markedly affect the relationship between fermentation and respiration of baker’s yeast in presence of glucose; (I) inhibits the 0 2 uptake, whilst (II) has little effect. Both compounds increase the rate of C02 formation, (II) having the greater action. The fermentation of fructose is similarly affected by (I). The 02 uptake and C02 output of
yeast in presence of glycerol are only slightly affected
by (I). S. S. Z.
Biochemical action of boron. II. Influence of boric acid on alcoholic fermentation and the production of lactic acid by yeast. J. V oicu and M. Nic u l e s c u (Bull. Soc. Chim. biol., 1932, 14, 1290— 1328).— The experiments are made using brewer’s yeast, baker’s yeast, and a commercial yeast prep, introduced into natural and synthetic media con
taining glucose or sucrose. The greater is the concn.
of carbohydrate the less is the inhibition produced by B(OH)3. With 5— 10% of carbohydrate the no. of yeast cells after the fermentation is the same in presence of 0-5% B(OH) 3 as in the control without B(OH)3; with 1% carbohydrate, however, the no.
of yeast-cells in the control is twice that in the medium containing B(OH)3. The ‘ inhibiting effect of B(OH) 3 varies with the p n of the media, being greater in acid than in alkaline or neutral solution.
In neutral solutions B(OH) 3 causes a decrease in EtOH, but an increase in volatile acid and glycerol formation;
no MeCHO or AcCOaH is, however, formed. In the presence of a little grape juice fermentation increases and lactic acid is formed. A. L .
Sterilisation of solutions of glucose and sucrose. W. B. Co o k (Iowa State Coll. J. Sei., 1932,
6, 417— 418).—A t room temp, yeast grows more rapidly in sucrose than in glucose-solutions, probably because at equal d the osmotic pressure in glucose is twice that in sucrose solution. A t 60° the death rate was higher in sucrose than in glucose solutions of equal d, probably because the osmotic pressure of the latter kept the hot H20 out of the cells. Addition of citric acid (0-02 or 0-0417) greatly accelerates the death of the yeast at 60°. Ch. Ab s.
Chemotaxis of plasmodia of M y x o in y c e te s . Y . Em oto (Proc. Imp. Acad. Tokyo, 1932, 8, 460—
463).— The chemotaxis towards various inorg. and org. substances at different vals. of pH and concn.
was investigated in Physarum viride and P. rigidum.
F. 0 . H.
Effect of strontium salts on the movements of P a r a m e c iu m ca u d a tu m . E. Eis e n b e r g-Ha m b u r g
(Arch. Protistenk, 1932,77,108— 124).— The rhythmic movement induced by Sr salts increased in rapidity with increasing concn. up to the toxic point, and declined with still higher concns. The accelerating effect was observed at all p n ranges examined, but the abs. rapidity of movement in a given concn. of Sr”
was greater in alkaline than in neutral media. Ba, Rb, and Cs salts produced similar but less definite results, and Ca, Mg, Na, K , Fe, and Cd salts were ineffective. An anion effect among the Sr salts is
was greater in alkaline than in neutral media. Ba, Rb, and Cs salts produced similar but less definite results, and Ca, Mg, Na, K , Fe, and Cd salts were ineffective. An anion effect among the Sr salts is