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Abnormal serum isoenzyme of leucine aminopeptidase (LAP) in malignant neoplastic disease

โœ Scribed by Roswell W. Phillips; Ernest R. Manildi


Publisher
John Wiley and Sons
Year
1974
Tongue
English
Weight
629 KB
Volume
34
Category
Article
ISSN
0008-543X

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โœฆ Synopsis


Leucine aminopeptidase (LAP) isoenzymes have been studied in the serum and urine of 53 consecutive patients with various types of malignant neoplastic disease, and compared with those in a group of 23 normal controls. Statistical evaluation and clinical correlation was made of the incidence and degree of zymogram abnormality and total serum and urine LAP levels in the patient group. LAP isoenzymes in normal sera separated into two principal fractions, one designated X, migrating in the alpha 2 globulin range, and Y, migrating in the beta globulin zone. Zymograms of the sera of patients with malignant neoplastic disease demonstrated a significant difference (p < 0,001) in the relative values of the X (aIpha 2) and Y (beta) fractions, compared to the normal controls. A progressive increase in the Y fraction developed in those whose neoplastic malignancy worsened. A decrease in peak height of the Y fraction occurred during periods of remission. The study suggests that the


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The colorimetric determination of leucin
โœ Julius A. Goldbarg; Alexander M. Rutenburg ๐Ÿ“‚ Article ๐Ÿ“… 1958 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 698 KB

HE FIRST demonstration of "leucylpepti-T dase" as a component of erepsin was made by measuring the rate of liberation of carboxyl groups from L-leucylglycine.6 However, since this substrate was hydrolyzed by enzymes other than leucylpeptidase, L-leucinamide, a more specific substrate was synthesized