Three-year efficacy of argon laser trabeculoplasty.

The authors report on the effect of argon laser trabeculoplasty on intraocular pressure (IOP) over a 3-year period with a mean follow-up period of 1.8 years in patients with uncontrolled primary open-angle glaucoma who had not undergone prior surgery. An analysis of the effect of laser trabeculoplasty using the criteria for success of an IOP of 22 mmHg or less with no further laser trabeculoplasty or glaucoma surgery, showed a cumulative success of 79% (112 eyes) at 1 year, 69% (85 eyes) at 2 years, and 59% (58 eyes) at 3 years. Similar results are presented for 22 eyes from patients with pseudoexfoliation glaucoma. The authors conclude that although the initial success rate of laser trabeculoplasty is high, it diminishes progressively over time.

Location of heme a on subunits I and II and copper on subunit II of cytochrome c oxidase.

A systemic study has been made of copper and heme a binding to subunits of beef heart cytochrome c oxidase. Copper and heme a were readily mobilized by ionic detergents, high ionic strengths, temperatures above 0 degrees C, thiol compounds, and gel-bound peroxides and free radicals when the subunits of the oxidase were dissociated from one another during polyacrylamide gel electrophoresis. Most subunits showed some affinity for heme a and copper under these conditions. However, in the presence of specific mixtures of ionic and nonionic detergents (e.g. 0.1% sodium dodecyl sulfate, 0.025% Triton X-100) at temperatures below 0 degrees C and in buffers of low ionic strength using 10 to 12% polyacrylamide gels preelectrophoresed for 3 days with thioglycolate, about 90% of the Cu was found on subunit II (Mr = 24,100), and heme a was found in equal amounts of subunits I (Mr = 35,800) and II. The oxidized-reduced and reduced-CO absorption spectra of these subunits resembled those of cytochrome c oxidase. It appears probable that in the native enzyme, subunit I contains heme a and subunit II contains copper and heme a. A relationship of mammalian cytochrome c oxidase to the two-subunit microbial cytochrome oxidase systems appears to exist.

The quaternary structure of an unusual high-molecular-weight intracellular haemoglobin from the bivalve mollusc Barbatia reeveana.

The arcid clam Barbatia reeveana contains an intracellular haemoglobin with an unusual structure. First, compared with other intracellular haemoglobins, it is extremely large, with a mol.wt. of 430000 and an s(20,w) of 13.6S. A minor component (mol.wt.=220000; s(20,w)=9.7S) is also present as a probable dissociation product of the major component. Secondly, this haemoglobin has an unusual subunit structure. It contains 1mol of haem per 16000g of protein, in common with most other haemoglobins. However, the smallest polypeptide that could be obtained after treatment with sodium dodecyl sulphate or 6m-guanidine with reducing agent has a mol.wt. of 32000-37000. Digestion of the haemoglobin with the proteinase subtilisin produces both 57000- and 30000-mol.wt. aggregates that contain 1mol of haem per 16000g of protein and that can be dissociated into 16500-mol.wt. polypeptides by treatment with sodium dodecyl sulphate. The intact polymer shows slight co-operativity (h=1.7), lacks a Bohr effect between pH7 and 8, and has a low oxygen affinity [P(50)=4.8kPa (36mmHg) at 20 degrees C] relative to other haemoglobins. The 30000-mol.wt. aggregate obtained by digestion of the polymer binds oxygen reversibly with an affinity greater than that of the polymer, but with some co-operativity (h=1.7). These results are consistent with the hypothesis that the subunits of this unusually large intracellular haemoglobin are 32000-mol.wt. polypeptides that in turn are composed of two covalently linked haem-containing oxygen-binding domains. This is the first report of an intracellular haemoglobin with such a structure.