The identification of sarcoplasmic reticulum terminal cisternae proteins in platelets. Biochem J 1989 Oct 15;263(2):605-8
Date
10/15/1989Pubmed ID
2512909Pubmed Central ID
PMC1133470DOI
10.1042/bj2630605Scopus ID
2-s2.0-0024426144 (requires institutional sign-in at Scopus site)Abstract
Two new proteins with apparent molecular masses of 53 kDa and 190 kDa have been identified in both sarcoplasmic reticulum and human blood platelets using a monoclonal antibody, FII1b5. The sarcoplasmic reticulum FII1b5 antigens were present in the terminal cisternae fraction, but were absent from light sarcoplasmic reticulum. The platelet and skeletal muscle proteins were not sensitive to digestion with endoglycosidase H under conditions that removed carbohydrate from the 53 kDa glycoprotein in sarcoplasmic reticulum or GPIIIa in platelet microsomes and did not bind 45Ca in a nitrocellulose overlay calcium-binding assay. These results distinguished the FII1b5 antigens from the 53 kDa glycoprotein and calsequestrin of sarcoplasmic reticulum. The 190 kDa platelet and sarcoplasmic reticulum proteins were extracted from membranes with high concentrations of NaCl, indicating that the high molecular mass FII1b5 antigens are peripherally associated with the bilayers. In contrast, the platelet and muscle 53 kDa proteins remained membrane-bound in the presence of high salt concentrations, suggesting that they are integral proteins.
Author List
Fischer TH, Barton DW, Krause KH, White TE, Campbell KP, White GC 2ndAuthor
Gilbert C. White MD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AcetylglucosaminidaseAnimals
Antibodies, Monoclonal
Blood Platelets
Blood Proteins
Calcium
Humans
Immunoblotting
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Membrane Proteins
Molecular Weight
Muscle Proteins
Muscles
Rabbits
Sarcoplasmic Reticulum
