PubMed · 905848
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J Lilien, R Rutz. 1977. A multicomponent model for specific cell adhesion.. https://pubmed.ncbi.nlm.nih.gov/905848/
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Latex plezoelectric immunoassay (LPEIA) is a new latex immunoassay using a plezoelectric quartz crystal (Kurosawa et al. Chem. Pharm. Bull. 1990, 38, 1117). This assay requires no immobilization of antigen or antibody on an electrode surface of a plezoelectric crystal, while the immobilization is indispensable for ordinary immunoassays using a plezoelectric crystal as a microbalance. The present paper improves a previous method (end-point analysis) by introducing the initial rate method using a batch cell; reduction of assay volume (1.2 mL) and shortening of assay time (2-3 min) were achieved. This assay was applied to the detection of antistreptolysin O antibody (ASO) in serum. The frequency change was proportional to the ASO concentration up to 1040 IU mL-1, and the method has good sensitivity for actual clinical application. The volume of serum required for the assay was 0.02 mL. Twenty-four clinical specimens were analyzed with this LPEIA, and the values obtained were compared with those obtained with a turbidimetric latex agglutination method. The correlation coefficient between these values was 0.950 (P < 0.01).
Monoclonal antibodies to human hemoglobin were produced and a colloidal gold agglutination method has been developed for detection of fecal occult blood. Since hemoglobin is composed of the tetramer, alpha 2 beta 2, a single monoclonal antibody-labeled colloidal gold can agglutinate with hemoglobin. The lowest detectable hemoglobin concentration was 0.5 micrograms/ml. A total of 785 fecal samples were determined using colloidal gold agglutination and compared with latex agglutination. The colloidal gold agglutination detected blood in 75 samples, whereas latex agglutination detected blood in 76 samples, and among them 70 were positive in both methods. Overall agreement between the two methods was 98%.
Alboaggregins (AL-A, AL-B, AL-C) isolated from Trimeresurus albolabris snake venom represent a new family of proteins which bind to platelet glycoprotein Ib (GPIb). These alboaggregins were purified to homogeneity with ion exchange HPLC (Mono-Q column) and hydrophobic HPLC (TSK Phenyl-5PW column). On SDS-polyacrylamide gel electrophoresis, apparent molecular weights of AL-A, AL-B and AL-C were 52 kDa, 26 kDa, and 121 kDa respectively, under nonreducing conditions. Upon reduction, each alboaggregin showed two types of chains with apparent molecular weights in the range of 15-20 kDa. All three alboaggregins agglutinated formalin-fixed platelets. Agglutination activities and binding of labeled alboaggregins to GPIb were specifically inhibited by the monoclonal antibody AK2 which is directed against the 45 kDa N-terminal region on GPIb, but not by monoclonal antibodies against other epitopes on GPIb. 125I-alboaggregin binding to platelets was not altered by the presence of thrombin. Alboaggregins did not bind to GPIIb/IIIa. Alboaggregins were competitive inhibitors for 125I-bovine vWF binding to platelets. Mutual competition studies between AL-A, AL-B and AL-C for the binding of labeled bovine vWF and AL-B to platelets demonstrated that AL-B and AL-C had a significantly higher affinity than AL-A.