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The laboratory. J Clin Pathol 66, 653-657 1976 ; . 7. Veith R, Perera C. Tricyclic antidepressanta.Engi J Med 300, N 504 1979 ; . Letter. 8. Kessler KM, Leech, Robin CC, Spann JF. Blood collection techniques, heparin and quinindine binding. Clin Pharmacol Ther 25, 204-210 1979 ; . 9. Fremstad D, Bergrud K. Plasma protein binding of drugs as influenced by blood collection methods. Acta Pharmacol Toxicol 39, 570-572 1976 ; . Letter. 10. Brog 0, Piafsky KM, Nilsen 00. Plasma bindingof basic drugs. Return to full-time student status. If the PEIA, in consultation with the medical director of the TPA-C, determines the diagnosis does not warrant continuous coverage under this provision, proper notice terminating the student status will be forwarded to the insured. The medical leave of absence is reviewed after a twelve-month period to verify if the dependent qualifies for a disability. If not, then COBRA election must occur for coverage to continue. Students, who voluntarily withdraw from school or have a lapse of coverage and later re-enroll as a fulltime student, may be reinstated for health benefit coverage; in this case, student health benefit coverage will become effective the first day of the month following the date of enrollment in the Plan and may be subject to pre-existing condition limitations. Working Families Tax Relief Act WFTRA ; of 2004 As a result of the Working Families Tax Relief Act WFTRA ; of 2004, the federal IRS has changed the way it treats children under the tax code. This change may affect you if you pay your health and life insurance premiums pre-tax through a Section 125 premium conversion plan. The IRS has developed a new definition for "qualified child" and "qualified relative." If you have dependents, they must meet one of these definitions to qualify for you to pay your premiums on a pre-tax basis. In nearly all circumstances, if your dependent meets PEIA eligibility criteria, they will also meet one of these federal definitions. The new definitions are as follows: A "qualifying child" QC ; is a child who: o o o has a specific, family-type relationship to the employee-taxpayer. Resides with the employee in his her household for more than half of the tax year with certain exemptions such as "temporary absences" if a full-time student ; . Is under age 19 and not a full-time student under age 24 if a full-time student ; as of the end of the calendar in which the employee's taxable year begins. There is no age requirement if a child is child is permanently and totally disabled.
Equilibrium bindingof human a-thrombin to heparin thrombin-proteinase reactions involves the binding of antiwas investigated at pH 7.4 as a function of thrombin thrombin to a unique pentasaccharide sequence in the heparin and heparin concentrations, NaCl concentration, tem- molecule 3-9 ; , which results in a conformational change in perature, and heparin chain length with the extrinsic inhibitor 10, ll ; . The the specific heparin pentasaccharide is fluorescence probe, p-aminobenzamidine, or by quan- alone sufficient to enhance the rate of inactivation of some titative affinity chromatography, in order to distinproteinases, such as factor Xa, whereas for other proteinases, guish between sequence-specific and nonspecific elec- such as thrombin, not only the pentasaccharide but also an trostatic modes of binding. Analysisof binding data by additional -13 saccharide residues are required for a signifia nonspecific binding model developed for proteincant heparin rate enhancement 4, 6, 12-14 ; . These observaor nucleic acid interactions, by the discrete binding site tions have been interpreted to mean that only antithrombin model previously used to analyze the thrombin-heparin interaction, indicated that both models described the binding to heparin is required to accelerate factor Xa of tion, whereas the binding of antithrombin together with the thrombin binding densities accessible to measurement. proteinase to heparin is necessary for heparin enhancement However, the strongdependence of the thrombin-hep- of thrombin inhibition. This conclusion is supported by: 1 ; the correspondence between the heparin chain length required arin bindinginteraction on NaCl concentration, its minimal dependence on temperature, and the increase to accelerate the thrombin-antithrombin reaction and that in apparent binding affinity with increasing heparin necessary to form a ternary complex in which thrombin and oligosaccharide chain length were best accounted for antithrombin are both bound to heparin 15 2 ; the progresby a nonspecific electrostatic association of thrombin sive loss in heparin rate enhancement for the thrombin, but with 5 to 6 anionic residues contained a 3-disaccha- not the factor Xareaction, at high concentrations of the in ride binding site heparin. This interaction was charof polysaccharide in a manner consistent with antithrombin and acterized by an intrinsic dissociation constant &, obs ; proteinase binding to separate heparin chains 7-9, 12, 16of p~ at physiological ionic strength. Although 18 and 3 ; the selective elimination of heparin's accelerating the nonspecific binding model satisfactorily described effect on the thrombin-antithrombin reaction by chemical the binding of thrombin to heparin chains ranging in modification of basic residues of thrombin presumably insize from 3 to -13 disaccharides in terms of a single volved in heparin binding 19, 20 ; . Based on this evidence, it intrinsic deviations this from model were aphas been postulated that the conformational change induced parent with longer heparin chains -22 to -35 disac- in antithrombin by binding to heparin makes antithrombin a charides ; from a progressive decrease in the intrinsic better inhibitor of factor Xa, whereas heparin enhances antiKD, obs up to 4-fold. Sedimentation equilibrium anal- thrombin inhibition of thrombin by approximation of the of yses of thrombin-heparin complexes suggested a secinhibitor and proteinase on the heparin surface. ond weakerbinding site on thrombinforheparin, Other investigators have suggested, however, that heparin which accounted for these deviations as well as the activation of antithrombin by an induced conformational observed insolubility of thrombin-heparin complexes change could suffice to explain heparin acceleration of all a t high thrombin binding densities. proteinase reactions. Thus, thenecessity for a longer heparin chain to accelerate thrombin inhibition has been rationalized by the larger heparin chain neutralizing positive charge in the The anticoagulant activity of the glycosaminoglycan hepa- proteinase-binding domain of antithrombin which otherwise rin derives from its ability to accelerate the inactivation of would result in an unfavorable interaction with the cationic blood coagulation proteinases by their primary inhibitoranti- thrombin, but not theanionic factor Xa 21 ; . Larger heparin thrombin I11 for reviews, see Refs. 1 and 2 ; . An important chains have also been suggested to induce a further conforfeature of the mechanism by which heparin accelerates anti- mational change in antithrombin which is necessary to promote a greater rate of reaction with thrombin 12, 22, 23 ; . * This work was supported by Grants HL-39888 from the National However, the observation that the extent the antithrombin of Institutes of Health to S. T Established Investigatorship of conformational change can be altered by chemical modificathe American Heart Association to S. T. and Swedish Medical Research Council Grant 4212 to I.B. ; . The costs of publication of tion without affecting heparin enhancement of the thrombinthis article were defrayed in part by the payment of page charges. antithrombin reaction rate hasargued against the antithromThis article must therefore be hereby marked "advertisement" in bin conformational change contributing significantly to hepaccordance with 18 U.S.C. Section 1734 solely to indicate this fact. arin acceleration of this reaction 24 ; . 3 whom correspondence should be addressed Div. of BiochemRapid kinetic studies have shown that heparin acceleration ical Res., EducationandResearch Bldg., Rm. 3126, HenryFord Hospital, 2799 W. Grand Blvd., Detroit, MI 48202. Tel.: 313-876- of the antithrombin-thrombin reaction results mainly from heparin binding to antithrombin promoting the binding of 3196.

Site F Synthetic Peptide: The overall strategy of these studieswas to prepare peptide 3371 fragments of apoB-100, to separateheparin-binding frag- 3352 ments by heparin-Sepharose affinity chromatography, to termine the structure of the heparin-binding fragments, and FIG.3. Synthetic peptides containing basic residues boxed ; to determine the relative heparin binding affinities of the in heparin-binding sites E and F. fragments. Two cleavage methods of differing specificity were chosen to avoid the possibility that one of the methods would preparative SDS-PAGE, and the isolated peptides shown in cleave within a heparin-binding region and destroy its hepa- lanes I, 2, 4-6, and 8 of Fig. 1B yielded sequence information rin-binding properties, thereby allowing the site to go unde- that allowed positioning of these fragments in the apoB-100 tected. The first method was a chemical cleavage with cyan- structure. The structure and placement of the isolated fragments ogen bromide at methionine residues of apoB-100; the second method involved enzymatic cleavage of LDL particles at within the deduced apoB-100 sequence 19-21 ; were established by amino-terminal sequence analysis in combination glutamic acid residues with S. aureus V-8 protease. Cyanogen bromide digestion of apoB-100 resulted in a large with the estimated molecular weight of the fragment, as number of fragments with molecular weights ranging from determined by SDS-PAGE, andthe specificity of the cleavage A. 5, 000 to 40, 000 Fig. l ; Because apoB-100 contains 78 method. The results of the fragment analysis are summarized methionine residues 19-21 ; , a complete digest would be ex- in Fig. 2, with the S. aureus V-8 protease fragments indicated pected to contain at least 79 fragments, not counting trypto- by an asterisk. Cyanogen bromide fragments of different phan cleavages and partial fragments. Approximately 15-20% lengths in the same region are the result of incomplete digesof the total digest bound to the affinity column. The peptide tion. In some instances, more than one peptide was contained pattern of the heparin-Sepharose-bound fragments was much within a given purified band. However, it was possible to less complex than that of the total digest approximately 12 determine the individual sequences because of the known major peptide bands ; , indicatingthat theaffinity column was sequence of apoB-100 19-21 ; . A sufficient number of seselective Fig. lA ; . Our approach was to isolate and charac- quence cycles were performed to allow unequivocal positionterize as many of the heparin-binding fragments as possible. ing of the amino terminus of each fragment. It should be The fragments were isolated by preparative SDS-PAGE; these emphasized that the assignment of the carboxyl terminus isolated fragments Fig. l A , lanes 1-9 ; represented the major relied heavily on the SDS-PAGE estimate of the molecular peptides in the bound fraction. In addition to the nine frag- weight; hence, it should be regarded as a best estimate rather ments shown in Fig. lA , six more cyanogen bromide fragments than a definitive one. In one case the cyanogen bromide were sequenced four were isolated from the group of frag- fragment beginning at residue 3308, Fig. 2 ; , we have not ments shown inFig. L4 with molecular weights less than assigned a carboxyl terminus because of evidence of glycosyl10, 000. ation of this fragment. During sequence analysis of this fragDigestion of apoB-100 on LDL with S. aureus V-8 protease ment, no signal was detected at the potential N-glycosylation also resulted in a complex mixture of fragments. In this case, sites at residues 3309 and 3331; therefore, there is some the molecular weights ranged from 5, 000 to 50, 000 Fig. 1B ; . question regarding the molecular weight of this fragment. Although the affinity-purified fraction contained asomewhat Sixteen heparin-binding cyanogen bromide fragments and simpler mixture that was enriched in several peptides, this seven S. aureus V-8 fragments were identified and positioned mixture was more complex than the bound fraction from in the apoB-100 sequence. As shown in Fig. 2, the fragments cyanogen bromide digestion. The fragments were purified by form six nonoverlapping sets. Within one set residues 5 and humalog.

This work was supported in part by the John S. Dunn Aesearch Foundation and the George Alfred Cook Memorial Fund

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