A homolog of acetylsalicylic acid, β -( o -ace-toxyphenyl)propionic acid, has been made successfully. Its toxicity and, analgesic properties have been determined on rats. It has been found to have analgesic properties in rheumatic patients. No free salicylic acid is eliminated in the urine. It appears that this compound does not exert its analgesic properties as a salicylate.

A homolog of acetylsalicylic acid, β-(o-ace-toxyphenyl)propionic acid, has been made successfully. Its toxicity and, analgesic properties have been determined on rats. It has been found to have analgesic properties in rheumatic patients. No free salicylic acid is eliminated in the urine. It appears that this compound does not exert its analgesic properties as a salicylate.

A method of analysis of urine for tartaric acid has been developed. A color comparison curve for the determination of tartaric acid in urine has been made for tartaric acid-metavanadate mixture. The metabolism of the different isomers of tartaric acid in a human being has been determined. The percentage of tartaric acid eliminated in the urine after intramuscular injection is only slightly greater than that after oral ingestion of tartaric acid. The D (-) isomer of tartaric acid is more readily metabolized than the L (+) isomer. The DL isomer taken by mouth gives slightly higher values in the urine than does the D (-) isomer, but it is considerably lower than the L (+) isomer.

The effect of sodium N-lauroyl sarcosinate and of sodium dehydroacetate on the activity of several enzymes was determined. These enzymes were salivary amylase, rennin, pancreatic trypsin, pancreatic lipase, and pancreatic amylase. The effect of LS and of DA dentifrices on the activity of salivary amylase was determined. The effect of salivary amylase activity immediately after brushing the teeth with several dentifrices was determined. The dentifrices included a LS dentifrice, a DA dentifrice, and a plain dentifrice. Also included was a plain mouthwash, a LS mouthwash, and a dry brush. The effect upon salivary amylase activity after brushing the teeth for one week with a LS dentifrice was determined. Some observations about the variability of human saliva are reported.

Lipolytic and proteolytic determinations have been made on unheated 5 per cent aqueous extracts of the three lots of cascara sagrada bark. Results of experimental work indicate that cascara sagrada possesses no significant lipolytic or proteolytic- like activity. Five per cent heated and unheated extracts of the 1951 lot of cascara sagrada bark showed no significant emulsin-like activity by a modification of the N. F. IX method for the assay of bitter almond oil for benzaldehyde. The hydrolytic agent has been isolated from the 1951 lot of cascara sagrada bark as an impure, light yellow-brown residue by a modified method for the isolation of lysozyme from egg white.

In considering the disintegration of enteric coatings of tablets it is essential to differentiate between intestinal contents and intestinal secretions. Enteric-coated tablets disintegrate in the intestinal contents which are seldom, if ever, alkaline. The disintegration of cellulose acetate phthalate and butyl stearate is due to the hydrolytic effect of the intestinal esterases and not, as is commonly believed, upon the alkalinity of the intestines.

Several factors influencing salivary amylase activity have been investigated and the results of the study are reported.

A method of analysis which can be used successfully to determine the lipolytic activity of Pancreatin, U. S. P., is presented.

Pancreatin U. S. P. contains the enzyme carboxypeptidase. It is a relatively stable enzyme. Pumpkin seed globulin serves as an excellent substrate for its analysis. Its activity may be expressed in terms of cc. of 0.02 N sodium hydroxide required to neutralize the amino acids produced from a definite amount of pumpkin seed alpba-globulin.

The official assay for pancreatic trypsin is not an assay for a single enzyme but for a mixture of proteolytic enzymes. Many samples labeled Pancreatin U. S. P. possess three times the minimum U. S. P. trypsin requirements. Triple-strength pancreatin is frequently no stronger than ordinary U. S. P. Pancreatin.

The age of the product does not determine its amylolytic activity. A good appearing pancreatin eleven years old had a higher amylase activity than an off-colored, but recently manufactured, product. The official definitions of pancreatin and extract of malt are misleading. The official definitions should give the time involved in the assays in order to give a truer picture of their enzymatic activities.