PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 48004

Correlation of the blood-level of a pregnancy-associated alpha-macroglobulin with the clinical course of cancer patients.

W H Stimson
View original source ↗Export metadata ↓

Abstract

The variations in serum level of a pregnancy-associated alpha-macroglobulin (P.A.M.) were studied during the treatment of breast-cancer patients. Good correlation was found between P.A.M. concentrations and the course of the disease--levels rose prior to the clinical recognition of metastatic disease and decreased significantly on successful treatment. Periodic P.A.M. determinations may allow detection of tumour recurrence while it is still at a treatable stage.

Explore related subjects

Alpha-GlobulinsBreast NeoplasmsFemaleHumansLymphatic MetastasisMacroglobulinsMastectomyMiddle AgedPostoperative CarePostoperative ComplicationsJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

W H Stimson. 1975-04-05. Correlation of the blood-level of a pregnancy-associated alpha-macroglobulin with the clinical course of cancer patients.. https://doi.org/10.1016/s0140-6736(75)92439-3

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1979

A rat serum glycoprotein whose synthesis rate increases greatly during inflammation.

Crossed immunoelectrophoresis of rat serum demonstrated considerably increased serum concentrations of at least ten different proteins during turpentine-induced inflammation. One protein, which moved during electrophoresis like an alpha 1 globulin, showed a particularly large increase. This protein was purified to homogeneity by ammonium sulfate fractionation followed by chromatography on DEAE-cellulose. Sephadex G-100, and concanavalin A-Sepharose, and finally disc electrophoresis in polyacrylamide gel. It has a molecular weight of 56,000 determined by equilibrium ultracentrifugation. An apparent molecular weight of 68,000 was estimated for the reduced protein by electrophoresis in polyacrylamide gel plus sodium dodecyl sulfate, suggesting that the native protein is composed of a single polypeptide chain. It has an E2801%, 1 cm of 5.2, an isoelectric pH of 4.7, and contains 19% carbohydrate. The protein does not inhibit bovine trypsin or chymotrypsin. Its physical properties and amino acid composition distinguish this protein from all other rat serum proteins hitherto characterized. During acute inflammation, induced 25 h previously, rats incorporated 20 times more [14C]leucine into this particular protein than did normal rats. However, incorporation into total serum protein during acute inflammation increased only slightly. Regardless of whether inflammation was induced by surgical injury or by a subcutaneous turpentine injection, within 48 h the serum concentration of this major acute-phase protein rose from the normal value of 0.46 g/liter to a maximum value of 7.2 g/liter, which constituted 10% of the total serum protein.

Alpha-Globulins↗