scholarly journals THE STARCH SUBSTRATE FILM METHOD FOR THE LOCALIZATION OF AMYLASE ACTIVITY SUGGESTIONS FOR A STANDARDIZED PROCEDURE

1973 ◽  
Vol 21 (2) ◽  
pp. 189-190 ◽  
Author(s):  
RICHARD J. SMITH ◽  
JACK FROMMER
Keyword(s):  
Amylase Activity ◽  
Starch Substrate ◽  
Film Method ◽  
Substrate Film

scholarly journals LOCALIZATION AND ONSET OF AMYLASE ACTIVITY IN MOUSE SALIVARY GLANDS DETERMINED BY A SUBSTRATE FILM METHOD

1971 ◽  
Vol 19 (5) ◽  
pp. 310-319 ◽  
Author(s):  
RICHARD J. SMITH ◽  
JACK FROMMER ◽  
ROBERT SCHIFF
Keyword(s):  
Parotid Gland ◽  
Salivary Glands ◽  
Amylase Activity ◽  
Submandibular Glands ◽  
Males And Females ◽  
Starch Substrate ◽  
Convoluted Tubules ◽  
Film Method ◽  
Positive Results ◽  
Substrate Film

A starch substrate film technique was used to determine the localization and onset of amylase activity in the major salivary glands of mice. The earliest activity occurred in the parotid gland of males and females at 8 days of age. The intensity of the reaction rapidly increased so that by day 16 the entire parotid gland was amylase-positive. The submandibular gland exhibited the sexual dimorphism that has been characterized for the adult gland. Amylase activity was observed in the male at 24 days of age, shortly after the first morphologic differences between the submandibular glands of males and females became apparent. The female showed positive results at 36 days of age. Amylase activity in the submandibular glands was localized to the convoluted tubules. As the gland developed, the amylase activity increased in correlation with the increasing concentration of these tubules. The sublingual gland was always amylase-negative.

scholarly journals Optimization, Purification, and Starch Stain Wash Application of Two Newα-Amylases Extracted from Leaves and Stems ofPergularia tomentosa

2017 ◽  
Vol 2017 ◽  
pp. 1-9 ◽  
Author(s):  
Imen Lahmar ◽  
Hanen El Abed ◽  
Bassem Khemakhem ◽  
Hafedh Belghith ◽  
Ferjani Ben Abdallah ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Enzyme Activity ◽  
Specific Activity ◽  
Amylase Activity ◽  
Detergent Industry ◽  
Sepharose Column ◽  
Stems And Leaves ◽  
Commercial Detergents ◽  
Starch Substrate

A continuous research is attempted to fulfil the highest industrial demands of natural amylases presenting special properties. Newα-amylases extracted from stems and leaves ofPergularia tomentosa, which is widespread and growing spontaneously in Tunisia, were studied by the means of their activities optimization and purification. Some similarities were recorded for the two identified enzymes: (i) the highest amylase activity showed a promoted thermal stability at 50°C; (ii) the starch substrate at 1% enhanced the enzyme activity; (iii) the twoα-amylases seem to be calcium-independent; (iv) Zn2+, Cu2+, and Ag2+were considered as important inhibitors of the enzyme activity. Following the increased gradient of elution on Mono Q-Sepharose column, an increase in the specific activity of 11.82-fold and 10.92-fold was recorded, respectively, for leaves and stems with the presence of different peaks on the purification profiles.Pergulariaamylases activities were stable and compatible with the tested commercial detergents. The combination of plant amylase and detergent allowed us to enhance the wash performance with an increase of 35.24 and 42.56%, respectively, for stems and leaves amylases. Characterized amylases were reported to have a promoted potential for their implication notably in detergent industry as well as biotechnological sector.

scholarly journals The distribution of acid and alkaline ribonuclease activities in preneoplastic and neoplastic rat livers.

1977 ◽  
Vol 25 (2) ◽  
pp. 115-121 ◽  
Author(s):  
S M Murthy ◽  
R Daoust
Keyword(s):  
Ribonucleic Acid ◽  
Serial Sections ◽  
Parenchymal Tissue ◽  
Precipitation Technique ◽  
Stromal Tissue ◽  
Alkaline Ribonuclease ◽  
Rat Livers ◽  
Film Method ◽  
Substrate Film

Ribonuclease (RNase) activities revealed by the substrate film method were compared with reactions for acid and alkaline RNase obtained by lead precipitation technique in serial sections of preneoplastic livers and hepatomas. The preneoplastic parenchymal tissue giving positive reactions with ribonucleic acid films showed both acid and alkaline RNase activities by lead precipitation technique, and the area of hyperplastic nodules nonreactive against substrate films were deficient in acid and alkaline RNase activities. Preneoplastic hyperbasophilic foci and hepatoma gave weak or negative reactions by either method, but necrotic areas and stromal tissue showed appreciable RNase activities. Thus a good correlation was observed in these tissues between the RNase activities revealed by the film method and those demonstrated by lead precipitation.

Automated Method for Determining Amylase Activity in Serum and Urine

1973 ◽  
Vol 19 (10) ◽  
pp. 1187-1192 ◽  
Author(s):  
A Mazzuchin ◽  
C Weggel ◽  
C J Porter
Keyword(s):  
Amylase Activity ◽  
Water Soluble ◽  
Standard Curve ◽  
The Past ◽  
Automated Method ◽  
Wide Range ◽  
On Line ◽  
Starch Substrate ◽  
Suspended Substrate

Abstract We describe an automated procedure for determination of α-amylase activity in serum or urine by use of a water-insoluble chromogenic starch substrate (commercially available). "AutoAnalyzer" (Technicon Corp.) equipment is used in which the sample and suspended substrate are introduced simultaneously into the flow system. After incubation at 37 °C the water-soluble blue-starch breakdown products are filtered on-line across a cellulose nitrate membrane. Absorbance is measured at 630 nm, and the α-amylase activity read from a standard curve. The automated procedure has been in use for the past year and has been found to be an operationally simple, reproducible, and reliable method, which can be applied over a wide range of enzyme activity. Results of comparative studies with other α-amylase methods are also described.

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