Comparative Studies of Mouse (H‐2) and Human (HL‐A) Histocompatibility Antigens

Abstract

A purification procedure applied to H-2 antigens (controlled by the H-2 locus) was used for the characterization of HL-A substances (HL-A2 and HL-A7) (controlled by the HL-A locus) solubilized from lymphoid cell membranes by delipidation. Upon Sephadex chromatography the serologically active material had an apparent M , of 32000, and displayed, in relation to H-2 antigens, a faster electrophoretic mobility and higher p l values. One sulfhydryl group and one (intrachain) disulfide bond were present in partially purified HL-A preparations. Reduction and aminoethylation in 4 M urea did not influence the electrophoretic migration of HL-A active substances, suggesting that, as already demonstrated for H-2 alloantigens, in HL-A molecules the genetic determinants are present on single polypeptide chains. Highly purified HL-A alloantigens, like H-2 substances, revealed a high degree of microheterogeneity. These findings further support the concept of the genetic and structural homology of the main histocompatibility systems in mouse and man.

Post‐translational phosphorylation affects the IgE binding capacity of caseins

“…Phosphate groups were released from caseins by acid and heat treatments [19]. Phosphate groups were determined as inorganic phosphates by a colorimetric method in a microtiter plate assay [20] based on the formation of a complex between phosphomolybdate and malachite green using previously described reagents [21,22].…”

Rapidly reversible flash‐induced electron transfer in a P‐700 chlorophyll—protein complex isolated with SDS

“…During the steps 5 and 6 all glassware was carefully rinsed with cone. HC1 to remove trace amounts of inorganic phosphate [8]. RNase T1 very strongly binds inorganic and organic phosphates and even if there is only a small amount of phosphate on the glass surface, the enzyme is accumulating phosphate during the isolation steps.…”

Synthesis and Evaluation of Novel [1,2,4]Triazolo[5,1‐c][1,2,4]‐triazines and Pyrazolo[5,1‐c][1,2,4]triazines as Potential Antidiabetic Agents

“…In a 96-well plate rabbit muscle glycogen phosphorylase (Sigma, USA) was incubated with test compounds and reaction mixture for 30 min. Phosphate was measured at 620 nm using Infinite M200 PRO microplate reader (Tecan), 20 min after the termination of the reaction with 150 mL of 1 M HCl containing 1.05% ammonium molybdate and 0.034% malachite green [56,58]. Test compound was replaced with 50 mM HEPES buffer (pH 8.0) in negative control experiments.…”